Isolation and structure of lamprey (Petromyzon marinus) insulin
Autor: | John H. Youson, W.M. Elliott, Erika M. Plisetskaya, Philip C. Andrews, H.G. Pollock |
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Rok vydání: | 1988 |
Předmět: |
Male
medicine.medical_specialty Swine medicine.medical_treatment Molecular Sequence Data Homology (biology) Islets of Langerhans Endocrinology Species Specificity Internal medicine biology.animal medicine Animals Insulin Amino Acid Sequence Amino Acids Agnatha Myxine glutinosa chemistry.chemical_classification biology Lamprey Fishes Lampreys biology.organism_classification Amino acid Petromyzon Biochemistry chemistry Sharks Female Animal Science and Zoology human activities Hagfish |
Zdroj: | General and Comparative Endocrinology. 69:46-55 |
ISSN: | 0016-6480 |
DOI: | 10.1016/0016-6480(88)90051-2 |
Popis: | Insulin has been purified to homogeneity from the caudal and cranial pancreas of the adult sea lamprey (Petromyzon marinus). The final yield was 18.6 nmol/g (127.8 micrograms/g). The structures of both A- and B-chains have been determined using amino acid analyses, gas-phase sequence analyses, and proteolytic mapping by fast atom bombardment-mass spectrometry. The sequence of the A-chain was found to be GIVEQCCHRKCSIYDMENYCN. The sequence of the B-chain, extended at the amino terminus, was determined to be SALT-GAGGTHLCGSHLVEALYVVCGDRGFFYTPSKT. Lamprey insulin retains the common features of vertebrate insulins. Sea lamprey insulin has no more homology to hagfish (Myxine glutinosa) insulin than it has to the teleost fish or to mammalian insulins. |
Databáze: | OpenAIRE |
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