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  • Amino Acid Sequence
  • American Association for the Advancement of Science (AAAS)  (17)
  • Annual Reviews
  • Blackwell Publishing Ltd
  • Institute of Physics
  • 1980-1984  (17)
  • 1930-1934
  • 1925-1929
  • 1980  (17)
Collection
Keywords
Publisher
  • American Association for the Advancement of Science (AAAS)  (17)
  • Annual Reviews
  • Blackwell Publishing Ltd
  • Institute of Physics
Years
  • 1980-1984  (17)
  • 1930-1934
  • 1925-1929
Year
  • 1
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    Bioactive conformation of luteinizing hormone-releasing hormone: evidence from a conformationally constrained analog (1980)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1980-11-07
    Description: An analog of luteinizing hormone-releasing hormone containing a gamma-lactam as a conformational constraint has been prepared with the use of a novel cyclization of a methionine sulfonium salt. The analog is more active as a luteinizing hormone-releasing hormone agonist that the parent hormone, and provides evidence for a bioactive conformation containing a beta-turn.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Freidinger, R M -- Veber, D F -- Perlow, D S -- Brooks, J R -- Saperstein, R -- New York, N.Y. -- Science. 1980 Nov 7;210(4470):656-8.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7001627" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Biological Assay ; Cells, Cultured ; Female ; *Gonadotropin-Releasing Hormone/analogs & derivatives ; Hydrogen Bonding ; Lactams ; Protein Conformation ; Rats ; Structure-Activity Relationship
    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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    Collagen: molecular diversity in the body's protein scaffold (1980)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1980-03-21
    Description: Intensive research in the last decade has revealed a wealth of detail on the mechanism of biosynthesis, molecular structure, and covalent cross-linking of collagen. Tissues of higher animals express a family of at least five genetically distinct types of collagen molecule, each apparently tailored for different construction work outside the cell. Within each genetic type of collagen, further chemical heterogeneity is also evident; the variations in hydroxylation, glycosylation, and cross-linking are dependent, for example, on tissue type, age, and hormonal status. The functional significance of collagen's molecular diversity and its control by different cells and tissues are not yet well understood but abnormalities of collagen in many human diseases keep this protein a focal molecule of medical research.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Eyre, D R -- New York, N.Y. -- Science. 1980 Mar 21;207(4437):1315-22.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7355290" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Calcification, Physiologic ; Cartilage/ultrastructure ; *Collagen/genetics/metabolism ; Epithelium/ultrastructure ; Extracellular Space/ultrastructure ; Humans ; Hydrogen Bonding ; Polymorphism, Genetic ; Protein Biosynthesis ; Protein Conformation ; Vertebrates
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  • 3
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    Comparison of the nucleic acid sequence of anglerfish and mammalian insulin mRNA's from cloned cDNA's (1980)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1980-12-19
    Description: Anglerfish (Lophius americanus) insulin complementary DNA was cloned in bacterial plasmids, and its sequence was determined. Fish insulin messenger RNA is larger (1.5 times) than the messenger RNA encoding mammalian (rat and human) insulin, in part because of a larger C peptide (an additional six amino acids or 18 nucleotides in length) but mainly because of increases in the 5' and 3' untranslated regions. Comparison of the fish, rat, and human insulin messenger RNA (from the complementary DNA) reveals that, in addition to the regions coding for the A and B peptides, sequence conservation is limited to a segment within the 5' untranslated region which may be involved in ribosomal binding, two small segments of the signal peptide, and two stretches of sequence in the 3' untranslated region.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hobart, P M -- Shen, L P -- Crawford, R -- Pictet, R L -- Rutter, W J -- AM 21344/AM/NIADDK NIH HHS/ -- New York, N.Y. -- Science. 1980 Dec 19;210(4476):1360-3.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7001633" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; *Biological Evolution ; Cloning, Molecular ; Codon ; Fishes/*genetics ; Insulin/*genetics ; Nucleic Acid Conformation ; Proinsulin/genetics ; Protein Biosynthesis ; Protein Precursors/genetics ; RNA, Messenger/*genetics
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  • 4
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    High-molecular-weight immunoreactive beta-endorphin in extracts of human placenta is a fragment of immunoglobulin G (1980)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1980-04-11
    Description: A high-molecular-weight protein with beta-endorphin- and adrenocorticotropin-immunoreactivities was isolated from extracts of human placenta after several purification steps, including immunoadsorption with a well-characterized antiserum raised to beta-endorphin. This protein was identified as the heavy chain of the human immunoglobulin class IgG1. These results have led to the recognition of homologies in the amino acid sequences of these physiologically unrelated molecules. They also suggest caution in accepting immunological competence as the sole criterion of the chemical identity of a ligand.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Julliard, J H -- Shibasaki, T -- Ling, N -- Guillemin, R -- New York, N.Y. -- Science. 1980 Apr 11;208(4440):183-5.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6244620" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Electrophoresis, Polyacrylamide Gel ; Endorphins/*analysis ; Female ; Humans ; Immunoglobulin G/*analysis ; Placental Extracts/*analysis ; Pregnancy ; Radioimmunoassay ; beta-Endorphin
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  • 5
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    Binding and factor XIIIa-mediated cross-linking of a 27-kilodalton fragment of fibronectin to Staphylococcus aureus (1980)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1980-08-22
    Description: A 27-kilodalton tryptic fragment, derived from the amino terminus of the 200-kilodalton fibronectin subunit, inhibited binding of intact fibronectin to Staphylococcus aureus and could be cross-linked to Staphylococcus aureus by blood coagulation Factor XIIIa. Interactions of fibronectin with Staphylococcus aureus via this fragment may be important for bacterial opsonization and attachment.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Mosher, D F -- Proctor, R A -- New York, N.Y. -- Science. 1980 Aug 22;209(4459):927-9.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7403857" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Factor XIII/*metabolism ; Fibronectins/*metabolism ; Humans ; Molecular Weight ; Opsonin Proteins ; Peptide Fragments ; Protein Binding ; Staphylococcus aureus/immunology/*metabolism ; Trypsin/metabolism
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  • 6
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    Ala-Gly- and Val-Asp-[Arg8]-vasopressin: bovine storage forms of arginine vasopressin with natriuretic activity (1980)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1980-02-22
    Description: Extracts of fresh-frozen bovine neurohypophysis were purified by chromatographic techniques to isolate and characterize the components that produce natriuresis in nondiuretic dogs. Two compounds with natiuretic properties similar to those of synthetic arginine vasopressin accounted for most of the natriuretic activity and appeared to be the prevalent vasopressin-like molecules in the extract. These peptides were Ala-Gly-[Arg8]-vasopressin and Val-Asp-[Arg8]-vasopressin; the natriuretic potency of each appeared to be similar to synthetic arginine vasopressin and could be observed with doses in the range of 50 picomoles. In the dog the most conspicuous difference between synthetic arginine vasopressin and the new vasopressin peptides was the smaller pressor responses to natriuretic doses of the new compounds.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Gitelman, H J -- Klapper, D G -- Alderman, F R -- Blythe, W B -- New York, N.Y. -- Science. 1980 Feb 22;207(4433):893-6.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7355269" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Arginine Vasopressin/analogs & derivatives/*metabolism/pharmacology ; Biological Assay ; Blood Pressure/drug effects ; Cattle ; Dogs ; Male ; Natriuresis/*drug effects ; Pituitary Gland, Posterior/*metabolism ; Protein Precursors/metabolism ; Structure-Activity Relationship
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  • 7
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    Phase variation: evolution of a controlling element (1980)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1980-09-19
    Description: Phase variation in bacteria is regulated by homologous recombination at a specific DNA site. This recombinational event causes the inversion of a 970-base-pair DNA sequence that includes the promoter necessary for transcription of a flagellar gene. The invertible segment is flanked by two sites that are necessary for the inversion and contains a gene (hin) whose product mediates the inversion event. The hin gene shows extensive homology with the TnpR gene carried on the Tn3 transposon. It is also homologous with the gin gene carried on bacteriophage mu. These relationships suggest that the phase variation system may have evolved by the association of a transposon with a resident gene and the subsequent specialization of these elements to regulate flagellar antigen expression.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Simon, M -- Zieg, J -- Silverman, M -- Mandel, G -- Doolittle, R -- New York, N.Y. -- Science. 1980 Sep 19;209(4463):1370-4.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6251543" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Bacterial Proteins/*genetics ; Base Sequence ; *DNA Transposable Elements ; DNA, Bacterial/genetics ; Flagellin/*genetics ; Genes ; Recombination, Genetic ; Salmonella/*genetics
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  • 8
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    Genetic variation in the human insulin gene (1980)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1980-08-01
    Description: Four recombinant lambda phages containing nucleotide sequences complementary to a cloned human preproinsulin DNA probe have been isolated from human DNA. Restriction analyses in conjunction with Southern hybridizations reveal two types of gene sequences. One isolate of each type was subjected to complete nucleotide sequence determination. The sequences contain the entire preproinsulin messenger RNA region, two intervening sequence. 260 nucleotides upstream from the messenger RNA capping site, and 35 nucleotides beyond the polyadenylate attachment site. Our results strongly suggest that these two gene types are allelic variants of a single insulin gene.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ullrich, A -- Dull, T J -- Gray, A -- Brosius, J -- Sures, I -- New York, N.Y. -- Science. 1980 Aug 1;209(4456):612-5.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6248962" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Cloning, Molecular ; *Dna ; DNA Restriction Enzymes ; DNA, Recombinant/metabolism ; *Genes ; Genetic Code ; *Genetic Variation ; Humans ; Insulin/*biosynthesis ; Nucleic Acid Hybridization ; Proinsulin/biosynthesis ; Rats ; Species Specificity
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  • 9
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    Newly made proteins zip through the cell (1980)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1980-01-11
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Marx, J L -- New York, N.Y. -- Science. 1980 Jan 11;207(4427):164-7.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7350651" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Binding Sites ; Cells/*metabolism ; Cytoplasmic Granules/metabolism ; Endoplasmic Reticulum/metabolism ; Glycoproteins/biosynthesis/metabolism ; Golgi Apparatus/metabolism ; Humans ; Lysosomes/metabolism ; Protein Precursors/metabolism ; Proteins/*metabolism
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  • 10
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    At least three human type alpha interferons: structure of alpha 2 (1980)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1980-09-19
    Description: The sequence of a human leukocyte-derived complementary DNA (cDNA), Hif-2h, which directs the formation in Escherichia coli of a polypeptide, IFN-alpha 1, with interferon (IFN) activity has been described. A second IFN cDNA, Hif-SN206, which also elicits synthesis of a biologically active IFN, IFN-alpha 2, is described in this article. Whereas IFN-alpha 2 is twice as active on human as on bovine cells, IFN-alpha 1 is 10 to 20 times more active on bovine than on human cells. As deduced from the cDNA's, the messenger RNA's for the two IFN's differ in length and in 20 percent of the nucleotides; the mature IFN polypeptides differ in 17 percent of the amino acids. Both IFN-alpha 1 and IFN-alpha 2 differ from the lymphoblastoid IFN described by others. Therefore, at least three different IFN-alpha genes are expressed in man; studies on genomic DNA reveal the presence of at least eight IFN-related genes.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Streuli, M -- Nagata, S -- Weissmann, C -- New York, N.Y. -- Science. 1980 Sep 19;209(4463):1343-7.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6158094" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; DNA, Recombinant ; Escherichia coli/genetics ; Genes ; Humans ; *Interferons/genetics ; Leukocytes ; Lymphocytes ; Mice ; RNA, Messenger/genetics ; Structure-Activity Relationship
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  • 11
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    Mouse interferons: amino terminal amino acid sequences of various species (1980)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1980-02-01
    Description: Mouse interferons of three size classes (A, 35,000 to 40,000 daltons; B, 26,000 to 33,000 daltons; and C, 20,000 daltons) were purified from Ehrlich ascites tumor cells infected with Newcastle disease virus. The sequences of the first 24 amino acids (No. 17 has not been identified) of interferons A and B are identical. The sequence of the first 20 amino acids of interferon C differs from that of A and B in 18 positions. There is partial homology in amino terminal sequence between mouse interferons A (or B) and a human fibroblast interferon and between mouse interferon C and a human lymphoblastoid interferon.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Taira, H -- Broeze, R J -- Jayaram, B M -- Lengyel, P -- Hunkapiller, M W -- Hood, L E -- New York, N.Y. -- Science. 1980 Feb 1;207(4430):528-30.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7352261" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Biological Evolution ; Carcinoma, Ehrlich Tumor/analysis ; Cells, Cultured ; Glycoproteins/analysis ; *Interferons/genetics ; Mice ; Molecular Weight
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  • 12
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    Calmodulin plays a pivotal role in cellular regulation (1980)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1980-01-04
    Description: The role of calcium ions (Ca2+) in cell function is beginning to be unraveled at the molecular level as a result of recent research on calcium-binding proteins and particularly on calmodulin. These proteins interact reversibly with Ca2+ to form a protein . Ca2+ complex, whose activity is regulated by the cellular flux of Ca2+. Many of the effects of Ca2+ appear to be exerted through calmodulin-regulated enzymes.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Cheung, W Y -- New York, N.Y. -- Science. 1980 Jan 4;207(4426):19-27.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6243188" target="_blank"〉PubMed〈/a〉
    Keywords: 3',5'-Cyclic-AMP Phosphodiesterases/metabolism ; Allosteric Regulation ; Amino Acid Sequence ; Animals ; Biological Evolution ; Calcium/*physiology ; Calcium-Binding Proteins/*physiology ; Calmodulin/*physiology ; Cell Communication ; Cyclic AMP/*physiology ; Enzyme Activation ; Phospholipases A/metabolism ; Protein Kinases/*metabolism ; Receptors, Drug/physiology ; Structure-Activity Relationship ; Troponin/physiology
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  • 13
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    Human fibroblast interferon: amino acid analysis and amino terminal amino acid sequence (1980)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1980-02-01
    Description: The purification of human fibroblast interferon has been simplified to a two-step procedure consisting of affinity chromatography on Blue Sepharose and sodium dodecyl sulfate polyacrlamide gel electrophoresis. A preliminary amino acid composition and the sequence of the 13 amino-terminal residues of homogeneous interferon prepared by this method is reported.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Knight, E Jr -- Hunkapiller, M W -- Korant, B D -- Hardy, R W -- Hood, L E -- New York, N.Y. -- Science. 1980 Feb 1;207(4430):525-6.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7352259" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Amino Acids/analysis ; Cells, Cultured ; Fibroblasts/*analysis ; Humans ; *Interferons
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  • 14
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    Acetylcholine receptor: complex of homologous subunits (1980)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1980-06-27
    Description: The acetylcholine receptor from the electric ray Torpedo californica is composed of five subunits; two are identical and the other three are structurally related to them. Microsequence analysis of the four polypeptides demonstrates amino acid homology among the subunits. Further sequence analysis of both membrane-bound and Triton-solubilized, chromatographically purified receptor gave the stoichiometry of the four subunits (40,000:50,000:60,000:65,000 daltons) as 2:1:1:1, indicating that this protein is a pentameric complex with a molecular weight of 255,000 daltons. Genealogical analysis suggests that divergence from a common ancestral gene occurred early in the evolution of the receptor. This shared ancestry argues that each of the four subunits plays a functional role in the receptor's physiological action.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Raftery, M A -- Hunkapiller, M W -- Strader, C D -- Hood, L E -- New York, N.Y. -- Science. 1980 Jun 27;208(4451):1454-6.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7384786" target="_blank"〉PubMed〈/a〉
    Keywords: Acetylcholine/metabolism ; Amino Acid Sequence ; Animals ; Electric Organ/*analysis ; Fishes ; Macromolecular Substances ; Molecular Weight ; Protein Conformation ; *Receptors, Cholinergic
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  • 15
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    Nucleotide sequence of human preproinsulin complementary DNA (1980)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1980-04-04
    Description: Recombinant bacterial plasmids that contain DNA complementary to human preproinsulin messenger RNA have been constructed. One clone contains the entire preproinsulin coding region, as well as the 3' untranslated region of the messenger RNA and eight nucleotides of the 5' untranslated region. Additional sequence information for the 5' untranslated region was obtained with the use of insulinoma messenger RNA in conjunction with specific primers from the cloned DNA for enzymatic chain termination sequence analysis. The results confirm the amino acid sequence of human proinsulin previously determined, and predict the amino acid sequence of the human preproinsulin signal peptide.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Sures, I -- Goeddel, D V -- Gray, A -- Ullrich, A -- New York, N.Y. -- Science. 1980 Apr 4;208(4439):57-9.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6927840" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Base Sequence ; Cloning, Molecular ; DNA, Recombinant ; Humans ; Insulin ; Nucleic Acid Hybridization ; Nucleotides/*genetics ; Proinsulin/*genetics ; Protein Precursors/*genetics ; RNA, Messenger/*genetics
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  • 16
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    Mouse immunoglobulin D: messenger RNA and genomic DNA sequences (1980)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1980-09-19
    Description: The molecular structure of a mouse immunoglobulin D from a plasmacytoma tumor and that of the normal mouse gene coding for immunoglobulin D are presented. The DNA sequence results indicate an unusual structure for the tumor delta chain in two respects: (i) Only two constant (C) region domains, termed C delta 1 and C delta 3 by homology considerations, are found; the two domains are separated by an unusual hinge region C delta H that lacks cysteine residues and thus cannot provide the covalent cross-links between heavy chains typically seen in immunoglobulins. The two domains and hinge are all coded on separate exons. (ii) At the carboxyl end of the delta chain there is a stretch of 26 amino acids that is coded from an exon located 2750 to 4600 base pairs downstream from the rest of the gene. Analogy with immunoglobulin M suggests that this distally coded segment C delta DC may have a membrane-binding function; however, it is only moderately hydrophobic. A fifth potential exon (C delta AC), located adjacent to the 3' (carboxyl) end of C delta 3, could code for a stretch of 49 amino acids. The tumor's expression of the delta gene may be aberrant, but the simplest interpretation would be that this tumor expresses one of the several biologically significant forms of the delta chain.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Tucker, P W -- Liu, C P -- Mushinski, J F -- Blattner, F R -- New York, N.Y. -- Science. 1980 Sep 19;209(4463):1353-60.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6968091" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; B-Lymphocytes/*immunology ; Base Sequence ; *Genes ; Glycoproteins/genetics ; Immunoglobulin Constant Regions/genetics ; Immunoglobulin D/*genetics ; Mice ; Myeloma Proteins/genetics ; RNA, Messenger/*genetics ; Receptors, Antigen, B-Cell/genetics ; Structure-Activity Relationship
    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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  • 17
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    Amino terminal sequence of the major component of human lymphoblastoid interferon (1980)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1980-02-01
    Description: Homogeneous human lymphoblastoid interferon with an apparent molecular size of 18,500 daltons was characterized by its amino acid composition. Analysis of the amino terminal sequence by Edman degradation indicates that the sequence is unique.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Zoon, K C -- Smith, M E -- Bridgen, P J -- Anfinsen, C B -- Hunkapiller, M W -- Hood, L E -- New York, N.Y. -- Science. 1980 Feb 1;207(4430):527-8.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7352260" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Amino Acids/analysis ; Cell Line ; Humans ; *Interferons ; Lymphocytes/*analysis
    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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