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  • Amino Acid Sequence
  • American Association for the Advancement of Science (AAAS)  (13)
  • Annual Reviews
  • Blackwell Publishing Ltd
  • Institute of Physics
  • 2000-2004
  • 1980-1984  (13)
  • 1930-1934
  • 1925-1929
  • 1982  (13)
Collection
Keywords
Publisher
  • American Association for the Advancement of Science (AAAS)  (13)
  • Annual Reviews
  • Blackwell Publishing Ltd
  • Institute of Physics
Years
  • 2000-2004
  • 1980-1984  (13)
  • 1930-1934
  • 1925-1929
Year
  • 1
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    alpha A-crystallin messenger RNA of the mouse lens: more noncoding than coding sequences (1982)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1982-02-19
    Description: The 14S messenger RNA (1300 to 1500 nucleotides) for the alpha A chain of alpha-crystallin of the mammalian lens is nearly three times larger than required to code for the polypeptide that contains 173 amino acids. As a means of accounting for this anomaly, a complementary DNA clone for the mouse alpha A-crystallin messenger RNA was constructed in pBR322 and sequenced. Derivation of the protein sequence from the nucleic acid sequence showed that mouse alpha A-crystallin is similar to that of other organisms. The messenger RNA contains 536 nucleotides located on the 3' side of the coding region, excluding the polyadenylate stretch. This 3' sequence does not encode any other crystallin and has multiple termination codons in the three possible reading frames.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉King, C R -- Shinohara, T -- Piatigorsky, J -- New York, N.Y. -- Science. 1982 Feb 19;215(4535):985-7.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7156978" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Cloning, Molecular ; Crystallins/*genetics ; Mice ; 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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  • 2
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    Complete amino acid sequence of urotensin I, a hypotensive and corticotropin-releasing neuropeptide from Catostomus (1982)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1982-10-08
    Description: Urotensin I, purified from extracts of the urophysis of a teleost fish (Catostomus commersoni), exhibits potent hypotensive activity (mammals and birds) and corticotropin-releasing activity (both fish and mammals). The primary structure of this 41-residue peptide was determined to be H-Asn-Asp-Asp-Pro-Pro-Ile-Ser-Ile-Asp-Leu-Thr-Phe-His-Leu-Leu-Arg-Asn-Met-Ile-Glu - Met-Ala-Arg-Ile-Glu-Asn-Glu-Arg-Glu-Gln-Ala-Gly-Leu-Asn-Arg-Lys-Tyr-Leu-Asp-Glu -Val-NH2. Extraction with 0.1N HCl at 100 degrees C cleaves the amino-terminal tripeptide, yeilding a fully active analog, urotensin I(4-41). The amino acid sequence was confirmed by measuring the biological activity of synthetic urotensin I(4-41). Urotensin I exhibits a striking sequence homology with ovine corticotropin-releasing factor and with frog sauvagine. These three peptides exhibit similar activities in biological test systems.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lederis, K -- Letter, A -- McMaster, D -- Moore, G -- Schlesinger, D -- New York, N.Y. -- Science. 1982 Oct 8;218(4568):162-5.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6981844" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Corticotropin-Releasing Hormone ; Fishes ; Peptides/*isolation & purification ; Species Specificity ; Urotensins/*isolation & purification
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
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  • 3
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    Somatic mutation in genes for the variable portion of the immunoglobulin heavy chain (1982)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1982-04-16
    Description: The size of the gene pool potentially encoding antibodies to p-azophenyl arsonate has been examined. A heavy chain-specific full-length complementary DNA clone has been constructed with the use of messenger RNA from a hybridoma that produces antibodies to the arsonate hapten and bears nearly a full complement of the determinants comprising the cross-reactive idiotype (CRI). The sequences of both the complementary DNA clone and the corresponding immunoglobulin heavy chain have been independently determined. A probe for the variable region gene was prepared from the original heavy chain complementary DNA clone and used to analyze, by Southern filter hybridization, genomic DNA from both A/J (CRI positive) and BALB/c (CRI negative) mice. Approximately 20 to 25 restriction fragments containing "germline" variable region gene segments were detected in both strains, and many are shared by both, Since 35 CRI-positive heavy chains have been partially sequenced thus far and 31 are different, the results of the hybridization analysis suggest that somatic mutation events involving the variable region gene segments of the heavy chain play a role in the origin of the amino acid sequence diversity seen in this system.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Sims, J -- Rabbitts, T H -- Estess, P -- Slaughter, C -- Tucker, P W -- Capra, J D -- A112127/PHS HHS/ -- AI-06020/AI/NIAID NIH HHS/ -- AI18016/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 1982 Apr 16;216(4543):309-11.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6801765" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Binding Sites, Antibody/*genetics ; Genes ; Haptens ; Immunoglobulin Heavy Chains/*genetics ; Immunoglobulin Idiotypes/genetics ; Immunoglobulin Variable Region/*genetics ; Mice ; *Mutation
    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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  • 4
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    Neuronal cell Thy-1 glycoprotein: homology with immunoglobulin (1982)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1982-05-14
    Description: The amino acid sequences of mouse brain Thy-1 glycoproteins are shown to be homologous to those of variable-region immunoglobulin domains. There is also good homology with constant domains and beta 2-microglobulin; overall the results suggest that Thy-1 may be like the primordial immunoglobulin domain. Preliminary evidence for an invertebrate Thy-1 homolog supports this possibility.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Williams, A F -- Gagnon, J -- New York, N.Y. -- Science. 1982 May 14;216(4547):696-703.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6177036" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Antigens, Surface/*immunology ; Antigens, Thy-1 ; Biological Evolution ; Epitopes ; Glycoproteins/*immunology ; Immunoglobulin Constant Regions/immunology ; Immunoglobulin Variable Region/immunology ; Immunoglobulins/*immunology ; Isoantibodies/biosynthesis ; Protein Conformation
    Print ISSN: 0036-8075
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  • 5
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    Hemoglobin Parchman: double crossover within a single human gene (1982)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1982-10-15
    Description: Structural analysis of a new variant hemoglobin revealed tryptic peptides with the amino acid composition of normal delta-globin, except for two internal peptides, which had the compositions of normal beta-globin. The most likely explanation for these findings is that a double, nonhomologous crossover between the delta-and beta-globin genes had occurred.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Adams, J G 3rd -- Morrison, W T -- Steinberg, M H -- New York, N.Y. -- Science. 1982 Oct 15;218(4569):291-3.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7123235" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Crossing Over, Genetic ; Globins/genetics ; Hemoglobins, Abnormal/*genetics ; Humans
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  • 6
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    Mammalian muscle acetylcholine receptor: a supramolecular structure formed by four related proteins (1982)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1982-12-17
    Description: The nicotinic acetylcholine receptor has been purified from fetal calf muscle. Amino terminal amino acid sequence data indicate that the mammalian receptor is formed from closely related but distinct subunits. A cytoskeletal component, actin, may be associated with the receptor.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Conti-Tronconi, B M -- Gotti, C M -- Hunkapiller, M W -- Raftery, M A -- GM-06965/GM/NIGMS NIH HHS/ -- NS-10294/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 1982 Dec 17;218(4578):1227-9.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7146904" target="_blank"〉PubMed〈/a〉
    Keywords: Actins/isolation & purification ; Amino Acid Sequence ; Animals ; Cattle ; Macromolecular Substances ; Molecular Weight ; Receptors, Cholinergic/*isolation & purification
    Print ISSN: 0036-8075
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  • 7
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    Nucleotide sequence of the p21 transforming protein of Harvey murine sarcoma virus (1982)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1982-09-03
    Description: Harvey murine sarcoma virus is a retrovirus which transforms cells by means of a single virally encoded protein called p21 has. We have determined the nucleotide sequence of 1.0 kilobase in the 5' half of the viral genome which encompasses the has coding sequences and its associated regulatory signals. The nucleotide sequence has identified the amino acid sequence of two additional overlapping polypeptides which share their reading frames and the carboxyl termini with p21 but which contain additional NH2-terminal amino acids.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Dhar, R -- Ellis, R W -- Shih, T Y -- Oroszlan, S -- Shapiro, B -- Maizel, J -- Lowy, D -- Scolnick, E -- New York, N.Y. -- Science. 1982 Sep 3;217(4563):934-6.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6287572" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Cell Transformation, Viral ; Cells, Cultured ; Defective Viruses/*genetics ; Genes, Viral ; Oncogene Protein p21(ras) ; Peptide Fragments ; Protein Biosynthesis ; Protein Conformation ; RNA, Viral/genetics ; Sarcoma Viruses, Murine/*genetics ; Viral Proteins/analysis/*genetics
    Print ISSN: 0036-8075
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  • 8
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    Rat pro-opiomelanocortin contains sulfate (1982)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1982-07-02
    Description: Intermediate lobes isolated from rat pituitary glands incorporated [35S]sulfate into pro-opiomelanocortin and other adrenocorticotropic hormone-containing peptides. Incubation of intermediate lobes in medium containing the arginine analog canavanine inhibited the cleavage of pro-opiomelanocortin into smaller products. Pro-opiomelanocortin that accumulated in the presence of canavanine was also sulfated.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hoshina, H -- Hortin, G -- Boime, I -- New York, N.Y. -- Science. 1982 Jul 2;217(4554):63-4.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6283633" target="_blank"〉PubMed〈/a〉
    Keywords: Adrenocorticotropic Hormone/*biosynthesis ; Amino Acid Sequence ; Animals ; In Vitro Techniques ; Kinetics ; Leucine ; Pituitary Gland/*metabolism ; Pituitary Hormones, Anterior/*biosynthesis ; Pro-Opiomelanocortin ; Protein Precursors/*biosynthesis ; Radioisotope Dilution Technique ; Rats ; Sulfur Radioisotopes ; Sulfuric Acids/*metabolism ; Tritium
    Print ISSN: 0036-8075
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  • 9
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    DNA sequence of a gene encoding a BALB/c mouse Ld transplantation antigen (1982)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1982-02-05
    Description: The sequence of a gene, denoted 27.5, encoding a transplantation antigen for the BALB/c mouse has been determined. Gene transfer studies and comparison of the translated sequence with the partial amino acid sequence of the Ld transplantation antigen establish that gene 27.5 encodes an Ld polypeptide. A comparison of the gene 27.5 sequence with several complementary DNA sequences suggests that the BALB/c mouse may contain a number of closely related L-like genes. Gene 27.5 has eight exons that correlate with the structural domains of the transplantation antigen.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Moore, K W -- Sher, B T -- Sun, Y H -- Eakle, K A -- Hood, L -- 1 T32 GM07616/GM/NIGMS NIH HHS/ -- GM 06965/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1982 Feb 5;215(4533):679-82.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7058332" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Cloning, Molecular/methods ; Genes ; H-2 Antigens/*genetics ; *Major Histocompatibility Complex ; Mice ; Mice, Inbred BALB C/*genetics ; Plasmids ; Repetitive Sequences, Nucleic Acid
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
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  • 10
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    Nonopiate effects of dynorphin and des-Tyr-dynorphin (1982)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1982-12-10
    Description: Intracerebroventricular administration of dynorphin produced potent and long-lasting effects on motor function and the electroencephalogram in rats. In addition, local iontophoretic or pressure ejection of dynorphin consistently inhibited hippocampal unit activity. None of these effects were significantly affected by naloxone even at high doses. Moreover, a fragment of dynorphin that failed to displace any of a number of tritiated narcotics from rat brain homogenates produced similar effects on these physiological measures in vivo. On the basis of a variety of criteria for "opiate action," the results suggest that a second biologically active site within the dynorphin sequence is capable of quite potent but nonopiate effects.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Walker, J M -- Moises, H C -- Coy, D H -- Baldrighi, G -- Akil, H -- 1F32DA04183/DA/NIDA NIH HHS/ -- DA02265/DA/NIDA NIH HHS/ -- New York, N.Y. -- Science. 1982 Dec 10;218(4577):1136-8.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6128791" target="_blank"〉PubMed〈/a〉
    Keywords: Action Potentials ; Amino Acid Sequence ; Animals ; Dynorphins ; Endorphins/*physiology ; Hippocampus/*physiology ; Male ; Pain/*physiopathology ; Rats ; Structure-Activity Relationship
    Print ISSN: 0036-8075
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  • 11
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    Herpes simplex virus type-1 glycoprotein D gene: nucleotide sequence and expression in Escherichia coli (1982)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1982-10-22
    Description: The protein coding region of the herpes simplex virus type-1 glycoprotein D (gD) gene was mapped, and the nucleotide sequence was determined. The predicted amino acid sequence of the gD polypeptide was found to contain a number of features in common with other virus glycoproteins. Insertion of this protein coding region into a bacterial expressor plasmid enabled synthesis in Escherichia coli of an immunoreactive gD-related polypeptide. The potential of this system for preparation of a type-common herpes simplex virus vaccine is discussed.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Watson, R J -- Weis, J H -- Salstrom, J S -- Enquist, L W -- New York, N.Y. -- Science. 1982 Oct 22;218(4570):381-4.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6289440" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Antigens, Viral/genetics ; Base Sequence ; Escherichia coli/genetics ; Gene Expression Regulation ; Genes ; Genes, Viral ; Glycoproteins/*genetics ; Peptides/genetics ; Protein Sorting Signals ; Simplexvirus/*genetics ; Viral Proteins/*genetics/immunology ; Viral Vaccines
    Print ISSN: 0036-8075
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  • 12
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    The carboxy terminus of the precursor to vasopressin and neurophysin: immunocytochemistry in rat brain (1982)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1982-08-27
    Description: A pituitary glycopeptide whose amino acid sequence was previously identified has now been recognized as the final portion of the precursor to arginine vasopressin and its associated neurophysin. Immunocytochemical techniques with antiserums against this 39 amino acid peptide and vasopressin were used to study their distribution in the rat central nervous system. The peptide is located in vasopressin-synthesizing cells in the neurosecretory magnocellular nuclei. Positively stained fibers project from the magnocellular nuclei through the median eminence to the posterior pituitary. Studies of the homozygous Brattleboro rat, which is known to be deficient in the production of vasopressin and its related neurophysin, also show the absence of immunoreactivity to this peptide. These immunocytochemical data strongly indicate that the peptide is synthesized with vasopressin.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Watson, S J -- Seidah, N G -- Chretien, M -- DA00154/DA/NIDA NIH HHS/ -- DA02265/DA/NIDA NIH HHS/ -- New York, N.Y. -- Science. 1982 Aug 27;217(4562):853-5.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6125034" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Arginine Vasopressin/*metabolism ; Brain/*metabolism ; Dynorphins ; Endorphins/metabolism ; Hypothalamus/metabolism ; Male ; Neurophysins/*metabolism ; Peptide Fragments ; Pituitary Gland, Posterior/metabolism ; Protein Precursors/analysis/*metabolism ; Rats ; Rats, Inbred Strains
    Print ISSN: 0036-8075
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  • 13
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    Growth hormone-releasing factor from a human pancreatic tumor that caused acromegaly (1982)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1982-11-05
    Description: A 44 amino acid peptide with growth hormone-releasing activity has been isolated from a human tumor of the pancreas that had caused acromegaly. The primary structure of the tumor-derived peptide is H-Tyr-Ala-Asp-Ala-Ile-Phe-Thr-Asn-Ser-Tyr-Arg-Lys-Val-Leu-Gly-Gln-Leu-Ser-Ala- Arg-Lys-Leu-Leu-Gln-Asp-Ile-Met-Ser-Arg-Gln-Gln-Gly-Glu-Ser-Asn-Gln-Glu-Arg-Gly -Ala-Arg-Ala-Arg-Leu-NH2. The synthetic replicate has full biological activity in vitro and in vivo specifically to stimulate the secretion of immunoreactive growth hormone. The tumor-derived peptide is identical in biological activity and similar in physiochemical properties to the still uncharacterized growth hormone-releasing factor present in extracts of hypothalamic tissues.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Guillemin, R -- Brazeau, P -- Bohlen, P -- Esch, F -- Ling, N -- Wehrenberg, W B -- AM-18811/AM/NIADDK NIH HHS/ -- HD-09690/HD/NICHD NIH HHS/ -- New York, N.Y. -- Science. 1982 Nov 5;218(4572):585-7.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6812220" target="_blank"〉PubMed〈/a〉
    Keywords: Acromegaly/*physiopathology ; Amino Acid Sequence ; Biological Assay ; Growth Hormone-Releasing Hormone/chemical synthesis/*isolation & purification ; Hormones, Ectopic/*isolation & purification ; Humans ; Pancreatic Neoplasms/*chemistry
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