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  • Amino Acid Sequence
  • American Association for the Advancement of Science (AAAS)  (19)
  • American Chemical Society (ACS)
  • 1975-1979  (19)
Collection
Keywords
Publisher
  • American Association for the Advancement of Science (AAAS)  (19)
  • American Chemical Society (ACS)
Years
Year
  • 1
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    Amino acid sequence homology between histone H5 and murine leukemia virus phosphoprotein p12 (1979)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1979-03-30
    Description: The amino terminal acid sequences of several mouse leukemia virus phosphoproteins (p12) show definite homology with the amino terminal conserved region of H5 histones, the phosphorylated nuclear proteins of nucleated erythrocytes. Differences in the amino acid compositions of the two groups of proteins seem to rule out the possibility that they evolved from a single common ancestral gene. The finding of sequence homology between viral p12's and cellular histones, however, is consistent with evolution of retrovirus structural proteins by a process of differentiation from preexisting cellular genes. The conserved primary and secondary structure at the amino terminal region, common to both groups of proteins, may be related to their common function of nucleic acid binding modulated by phosphorylation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Henderson, L E -- Gilden, R V -- Oroszlan, S -- New York, N.Y. -- Science. 1979 Mar 30;203(4387):1346-8.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/218289" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Carrier Proteins ; Cell Nucleus/analysis ; Chickens/blood ; Erythrocytes/analysis ; Geese/blood ; *Histones ; Leukemia Virus, Murine/*analysis ; Nucleic Acids/metabolism ; *Phosphoproteins ; Structure-Activity Relationship ; *Viral Proteins
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 2
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    Specific nonopiate receptors for beta-endorphin (1979)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1979-09-07
    Description: Iodinated beta H-[2-D-alanine]endorphin exhibits specific binding to cultured human lymphocytes. The binding is inhibited by low concentrations of beta-endorphin and its D-alanine derivative, but is not affected by opiate agonists and antagonists, or by enkephalin analogs, beta-lipotropin, adrenocorticotrophic hormone, or alpha-melanocyte-stimulating hormone; this suggests the existence of a specific, non-opiate binding site (receptor) for beta-endorphin. The carboxy-terminal region of beta-endorphin is essential for this binding activity, since alpha-endorphin is not active. beta-Endorphin may be a circulating hormone with peripheral physiological effects that are not primarily mediated through interactions with opiate or enkephalin receptors.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hazum, E -- Chang, K J -- Cuatrecasas, P -- New York, N.Y. -- Science. 1979 Sep 7;205(4410):1033-5.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/224457" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Cells, Cultured ; Endorphins/blood/*metabolism ; Humans ; Lymphocyte Activation ; Lymphocytes/*metabolism ; Receptors, Drug/*metabolism ; Receptors, Opioid/metabolism ; Stress, Physiological/metabolism ; Structure-Activity Relationship
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  • 3
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    Fibrinopeptide B and aggregation of fibrinogen (1979)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1979-04-13
    Description: Removal of fibrinopeptide B from human fibrinogen by reaction with the procoagulant enzyme from copperhead snake venom below 25 degrees C resulted in tight aggregation of the fibrinogen, which, in turn, progressively blocked a concomitant but sluggish release of fibrinopeptide A by the enzyme. When the clots obtained at less than 25 degrees C were warmed, they dissociated into soluble aggregates and monomers. Release of fibrinopeptide A then resumed, and a secondary coagulation followed. The aggregation induced by release of fibrinopeptide B itself involves a plasmin-susceptible segment located just distal to B in the B beta chain of fibrinogen, a segment previously shown to be of little importance in the aggregation induced by release of fibrinopeptide A.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Shainoff, J R -- Dardik, B N -- New York, N.Y. -- Science. 1979 Apr 13;204(4389):200-2.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/155308" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Binding Sites ; Crotalid Venoms/*metabolism ; Fibrinogen/*metabolism ; Fibrinolysin/metabolism ; Fibrinopeptide A/metabolism ; Fibrinopeptide B/*metabolism ; Humans ; Molecular Weight ; Protein Binding ; Temperature
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  • 4
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    beta-Galactosidase and selective neutrality (1979)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1979-03-09
    Description: Three hypotheses to explain the amino acid composition of proteins are inconsistent (P congruent to 10(-9) with the experimental data for beta-galactosidase from Escherichia coli. The exceptional length of this protein, 1021 residues, permits rigorous tests of these hypotheses without complication from statistical artifacts. Either this protein is not at compositional equilibrium, which is unlikely from knowledge about other proteins, or the evolution of this protein and its coding gene have not been selectively neutral. However, the composition of approximately 60 percent of the molecule is consistent with either a selectively neutral or nonneutral evolutionary process.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Holmquist, R -- New York, N.Y. -- Science. 1979 Mar 9;203(4384):1012-4.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/106468" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Amino Acids/analysis ; Base Sequence ; Biological Evolution ; Escherichia coli/enzymology ; Galactosidases/*genetics ; Genes ; Genetic Code ; *Selection, Genetic ; beta-Galactosidase/analysis/*genetics
    Print ISSN: 0036-8075
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  • 5
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    Beta-galactosidase and selective neutrality (1979)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1979-10-12
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Holmquist, R -- Conroy, T -- New York, N.Y. -- Science. 1979 Oct 12;206(4415):235.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/113875" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Escherichia coli/*genetics ; Galactosidases/*genetics ; Probability ; Selection, Genetic ; beta-Galactosidase/*genetics
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
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  • 6
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    Organization of the immune response genes (1979)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1979-10-19
    Description: The I region of the major histocompatibility complex contains immune response genes that display considerable polymorphism; that is, there are many alleles at each locus. These genes regulate the immune response to antigen by mediating intercellular communication among lymphoreticular cells. An analysis of the primary structure of the products of two subregions of (I-A, I-E/C) was undertaken in order to understand the genetic organization of the region, the evolution of the genes and, eventually, their function.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Uhr, J W -- Capra, J D -- Vitetta, E S -- Cook, R G -- New York, N.Y. -- Science. 1979 Oct 19;206(4416):292-7.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/113876" target="_blank"〉PubMed〈/a〉
    Keywords: Alleles ; Amino Acid Sequence ; Antigens, Surface/analysis/*genetics ; *Cell Communication ; *Genes, MHC Class II ; *Immunity, Cellular ; Lymphocytes/immunology ; Macromolecular Substances ; Macrophages/immunology ; Molecular Weight ; Polymorphism, Genetic
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  • 7
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    A synthetic pentapeptide with biological activity characteristic of the thymic hormone thymopoietin (1979)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1979-06-22
    Description: The pentapeptide arginyl-lysyl-aspartyl-valyl-tyrosine, corresponding to amino acid residues 32--36 in thymopoietin, was synthesized. In vitro, this pentapeptide induced the differentiation of murine prothymocytes to thymocytes and inhibited differentiative induction of cells of the B lineage. This combination of actions is presently unique to the parent molecule thymopoietin. In vivo, the pentapeptide reduced the high numbers of autologous rosette-forming cells normally present in the spleens of athymic mice; this also is a property of thymopoietin. These results suggest that this readily synthesized pentapeptide corresponds to an active site of thymopoietin and might serve as a therapeutic substitute for thymopoietin.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Goldstein, G -- Scheid, M P -- Boyse, E A -- Schlesinger, D H -- Van Wauwe, J -- New York, N.Y. -- Science. 1979 Jun 22;204(4399):1309-10.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/451537" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Antigens, Surface/analysis ; Cell Differentiation/drug effects ; Complement System Proteins ; Isoantigens/analysis ; Lymphocytes/cytology/*immunology ; Mice ; Mice, Nude/immunology ; Oligopeptides/chemical synthesis/*pharmacology ; Receptors, Drug/analysis ; Structure-Activity Relationship ; Thymopoietins/*pharmacology ; Thymus Hormones/*pharmacology
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  • 8
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    Experimental phenylketonuria: replacement of carboxyl terminal tyrosine by phenylalanine in infant rat brain tubulin (1979)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1979-10-26
    Description: In the brains of newborn rats, about half of the tubulin molecules are modified posttranslationally by the addition of an aromatic amino acid at the carboxyl terminus of the alpha chain. Of the added residues, 96 percent are tyrosine and 4 percent are phenylalanine. After induction of hyperphenylalaninemia, the proportion of tubulin molecules containing carboxyl terminal phenylalanine increases up to eightfold and the pool of tyrosine-containing molecules decreases by an equivalent amount.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Rodriguez, J A -- Borisy, G G -- New York, N.Y. -- Science. 1979 Oct 26;206(4417):463-5.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/574315" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Brain/*metabolism ; Cytoplasm/metabolism ; *Disease Models, Animal ; Humans ; Microtubules/metabolism ; Phenylalanine/*metabolism ; Phenylketonurias/*metabolism ; Protein Binding ; Rats ; Tubulin/*metabolism ; Tyrosine/metabolism
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  • 9
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    Protein and nucleic acid sequence data and phylogeny (1979)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1979-09-07
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Demoulin, V -- New York, N.Y. -- Science. 1979 Sep 7;205(4410):1036-9.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/472727" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Cytochromes/genetics ; Ferredoxins/genetics ; *Phylogeny ; Proteins/*genetics ; RNA, Ribosomal/*genetics
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  • 10
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    The major histocompatibility complex of the mouse (1979)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1979-02-09
    Description: Like physicists striving to develop a unified field theory, immunologists are attempting to bring order to the microcosmos of defense reactions. Indications are that one of the most important constants in this microcosmos is the major histocompatibility complex (MHC) of the species. A test of any interpretation of the MHC's role in immunity is how well it explains this system's polymorphism. One of the most crucial questions an MHC hypothesis must answer is: Why are there so many alleles at this complex?〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Klein, J -- New York, N.Y. -- Science. 1979 Feb 9;203(4380):516-21.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/104386" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Binding Sites ; Blood Proteins/genetics ; Genes ; *Genes, MHC Class II ; Genetic Linkage ; H-2 Antigens/*genetics ; Lymphocytes/immunology ; *Major Histocompatibility Complex ; Mice/*immunology ; Phenotype ; Polymorphism, Genetic
    Print ISSN: 0036-8075
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  • 11
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    Human growth hormone: complementary DNA cloning and expression in bacteria (1979)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1979-08-10
    Description: The nucleotide sequence of a DNA complementary to human growth hormone messenger RNA was cloned; it contains 29 nucleotides in its 5' untranslated region, the 651 nucleotides coding for the prehormone, and the entire 3' untranslated region (108 nucleotides). The data reported predict the previously unknown sequence of the signal peptide of human growth hormone and, by comparison with the previously determined sequences of rat growth hormone and human chorionic somatomammotropin, strengthens the hypothesis that these genes evolved by gene duplication from a common ancestral sequence. The human growth hormone gene sequences have been linked in phase to a fragment of the trp D gene of Escherichia coli in a plasmid vehicle, and a fusion protein is synthesized at high level (approximately 3 percent of bacterial protein) under the control of the regulatory region of the trp operon. This fusion protein (70 percent of whose amino acids are coded for by the human growth hormone gene) reacts specifically with antibodies to human growth hormone and is stable in E. coli.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Martial, J A -- Hallewell, R A -- Baxter, J D -- Goodman, H M -- New York, N.Y. -- Science. 1979 Aug 10;205(4406):602-7.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/377496" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Cattle ; DNA, Recombinant/*metabolism ; Escherichia coli/*metabolism ; Growth Hormone/*biosynthesis ; Humans ; Pituitary Gland/metabolism ; Pituitary Neoplasms/metabolism ; *Plasmids ; Poly A/metabolism ; Prolactin/biosynthesis ; *Protein Biosynthesis ; RNA, Messenger/metabolism ; *Transcription, Genetic
    Print ISSN: 0036-8075
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  • 12
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    alpha1-Antitrypsin: the presence of excess mannose in the Z variant isolated from liver (1978)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1978-09-29
    Description: The Z variant of alpha1-antitrypsin was isolated by a new technique from the liver of a patient homozygous for the Z allele of the protease inhibitor locus. The material was homogenous and antigenically competent but had no protease inhibiting capacity. An interesting correlation was found between the subcellular localization and the carbohydrate composition of the Z variant from liver. Carbohydate analysis of this glycoprotein showed an absence of galactose and sialic acid, an appreciable decrease in N-acetylglucosamine, and an almost twofold increase in mannose residues. These data indicate a considerable slowdown in the processing of the oligosaccharides of liver Z variant. In spite of the absence of sialyl residues, the liver Z varant was microheterogeneous by analytical isoelectric focusing. The isoproteins of liver Z variant coincided with those of asialo M variant in the focusing field.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hercz, A -- Katona, E -- Cutz, E -- Wilson, J R -- Barton, M -- New York, N.Y. -- Science. 1978 Sep 29;201(4362):1229-32.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/308696" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Carbohydrate Metabolism ; Female ; Galactose/metabolism ; Glycoproteins/genetics ; Homozygote ; Humans ; Liver/metabolism ; Mannose/metabolism ; Middle Aged ; Mutation ; Phenotype ; Sialic Acids/metabolism ; alpha 1-Antitrypsin/*genetics/metabolism
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  • 13
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    Origins of prokaryotes, eukaryotes, mitochondria, and chloroplasts (1978)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1978-01-27
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Schwartz, R M -- Dayhoff, M O -- New York, N.Y. -- Science. 1978 Jan 27;199(4327):395-403.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/202030" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Base Sequence ; *Biological Evolution ; *Cells ; *Chloroplasts ; Computers ; Cytochrome c Group ; *Eukaryotic Cells ; Ferredoxins ; *Mitochondria ; Nucleic Acids ; *Prokaryotic Cells ; Proteins ; RNA, Ribosomal
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  • 14
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    Invertebrate collagens (1978)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1978-11-10
    Description: The collagens of all major invertebrate phyla have been studied, but characterization has been thorough in only a few classes and in no case in the detail (such as sequence analysis) known for vertebrate collagen. Biochemical data on insect collagen are particularly sparse. Invertebrate and vertebrate collagens are strikingly similar, with some notably unique features in annelids and nematodes. Present data do not support the suggestion that invertebrate collagens resemble vertebrate basement membrane collagen. In invertebrates, as in vertebrates, collagens of specific tissues show differenes that probably reflect individual tissue requirements.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Adams, E -- New York, N.Y. -- Science. 1978 Nov 10;202(4368):591-8.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/212833" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Carbohydrates/analysis ; Collagen/*analysis ; Glycoproteins/analysis ; Invertebrates/*analysis/enzymology ; Macromolecular Substances ; Molecular Weight ; Polymorphism, Genetic ; Procollagen-Proline Dioxygenase/metabolism ; Species Specificity
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  • 15
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    Electrostatic effects in proteins (1978)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1978-09-29
    Description: Electrostatic effects dominate many aspects of protein behavior. When polypeptide chains fold up, most polar side chains seek the exterior, where they can be solvated. Water bound in the interior has been found between the domains of enzymes of the chymotrypsin family, and between the subunits of hemoglobin and tobacco mosaic virus protein. Assembly of this protein from disk to virus is triggered by electrostatic interactions between neighboring subunits. Lysozyme stabilizes the constellation of charges involved in the transition state of its substrate by both permanent and induced dipoles. All factors that lower the oxygen affinity of hemoglobin act by strengthening the salt bridges that constrain its quaternary deoxy (T) structure. Enzymes of thermophile bacteria owe their extra stability mostly to additional salt bridges. The rate of denaturation of hemoglobins by alkali is determined by the ionization of internal side chains with pK's of about 12.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Perutz, M F -- New York, N.Y. -- Science. 1978 Sep 29;201(4362):1187-91.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/694508" target="_blank"〉PubMed〈/a〉
    Keywords: Allosteric Regulation ; Amino Acid Sequence ; Catalysis ; Ions ; Macromolecular Substances ; Protein Conformation ; Protein Denaturation ; *Proteins ; Salts ; Structure-Activity Relationship ; Temperature ; Viruses/ultrastructure ; Water
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  • 16
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    Vasopressin analog with extraordinarily high antidiuretic potency: a study of conformation and activity (1978)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1978-01-20
    Description: Application of information derived from a three-dimensional model of vasopressin bound to its antidiuretic receptor has resulted in the design and synthesis of a potent analog, [1-deamino, 2-phenylalanine, 7-(3,4-dehydroproline)]-arginine vasopressin; this analog has a specific antidiuretic activity of 13,000 +/- 1,250 units per milligram; noteworthy at these doses is the absence of any detectable pressor activity. Three modifications based on conformational considerations were introduced into the vasopressin molecule in preparing the analog: (i) to enhance binding, a double bond was introduced into the side chain of an amino acid residue occupying a corner position of a beta turn in the vasopressin conformation, (ii) the hydroxyl moiety was deleted from Tyr2, and (iii) to tighten the backbone structure and to enhance the enzymatic resistance of the analog, the NH2-terminal amino group was deleted.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Smith, C W -- Walter, R -- New York, N.Y. -- Science. 1978 Jan 20;199(4326):297-9.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/619455" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Deamino Arginine Vasopressin/analogs & derivatives ; Diuresis/drug effects ; Heart Rate/drug effects ; Protein Conformation ; Structure-Activity Relationship ; Vasopressins/*analogs & derivatives/pharmacology
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  • 17
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    Aspects of hypothalamic regulation of the pituitary gland (1978)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1978-10-06
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Schally, A V -- New York, N.Y. -- Science. 1978 Oct 6;202(4363):18-28.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/99816" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Awards and Prizes ; Gonadotropin-Releasing Hormone/isolation & purification/physiology ; Hormones/pharmacology ; Hypothalamic Hormones/*physiology ; Hypothalamus/*physiology ; Pituitary Gland, Anterior/*physiology ; Somatostatin/isolation & purification/physiology ; Structure-Activity Relationship ; Thyrotropin-Releasing Hormone/isolation & purification
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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  • 18
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    Amino acid sequence of the Fc region of a canine immunoglobulin M: interspecies homology for the IgM class (1978)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1978-06-09
    Description: The amino acid structure for the Fc portion of a canine immunoglobulin mu chain was determined. The sequence was compared with those of two human mu chains, and a high degree of interspecies homology was observed. The preservation of primary structure between species is probably reflective of the unique functions associated with the immunoglobulin M class.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wasserman, R L -- Capra, J D -- New York, N.Y. -- Science. 1978 Jun 9;200(4346):1159-61.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/653360" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Biological Evolution ; Dogs ; Humans ; *Immunoglobulin Fc Fragments ; *Immunoglobulin M ; Species Specificity
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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  • 19
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    Cloning human fetal gamma globin and mouse alpha-type globin DNA: characterization and partial sequencing (1978)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1978-12-22
    Description: Two globin-related clones isolated from collections of bacteriophages containing unfractionated Eco RI fragments of human and mouse DNA were characterized. Charon3AHs51.1Hbgamma includes 2.7 kilobase pairs of human DNA containing a large part of a fetal gamma globin chain structural gene; Charon 3AMm30.5 includes 4.7 kilobase pairs of mouse DNA related to alpha globin. The human fetal gamma globin gene has within its coding region two intervening sequences of noncoding DNA, IVS 1 and IVS 2, of approximately 1-0 and 900 base pairs. Sequence IVS 1 is located at the position of one of the two intervening sequences occurring in adult globin genes; IVS 2 is located at the position of the other.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Smithies, O -- Blechl, A E -- Denniston-Thompson, K -- Newell, N -- Richards, J E -- Slightom, J L -- Tucker, P W -- Blattner, F R -- New York, N.Y. -- Science. 1978 Dec 22;202(4374):1284-9.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/725604" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Codon ; DNA Restriction Enzymes/metabolism ; DNA, Recombinant ; Fetal Hemoglobin/*genetics ; *Genes ; Globins/*genetics ; Humans ; Methods ; Mice ; Nucleic Acid Hybridization ; RNA, Messenger/genetics
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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