Properties of immunoreactive glucagon fractions of canine stomach and pancreas.

作者: C B Srikant , K McCorkle , R H Unger

DOI: 10.1016/S0021-9258(18)71834-6

关键词:

摘要: Abstract The present study was designed to identify the physicochemical, immunologic, and biologic properties of immunoreactive glucagon (IRG) moieties canine gastric fundus compare them with those pancreas. Acid-alcohol extracts pancreas dogs were subjected Bio-Gel P-10 chromatography, elution profiles both organs revealed IRG peaks in Mr = 2,000 3,500, 9,000 zones; extracts, a void volume peak also present. On basis Sephadex G-150 rechromatography sucrose density gradient ultracentrifugation latter estimated have 65,000. Incubation fundic IRG65,000 8 M urea failed alter its position. Its pI 6.4, while IRG3,500 had 6.15 pancreatic 6.25.Fundic IRG9,000 4.5 4.65. Dilution curves these three two IRGs parallel crystalline beef-pork glucagon. glycogenolytic activity IRG65,000, measured isolated rat liver system, not different from that immunoequivalent amounts dog or Both devoid lacker adenylate cyclase stimulating 125I-glucagon displacing when tested on partially purified membranes. Fundic however, stimulated displaced same degree as more active than activity. This clearly attributable differences binding cell

参考文章(19)
Earl W. Sutherland, Christian. de Duve, Origin and distribution of the hyperglycemic-glycogenolytic factor of the pancreas. Journal of Biological Chemistry. ,vol. 175, pp. 663- 674 ,(1948) , 10.1016/S0021-9258(18)57183-0
Demetra Rigopoulou, Isabel Valverde, Jose Marco, Gerald Faloona, Roger H. Unger, Large glucagon immunoreactivity in extracts of pancreas. Journal of Biological Chemistry. ,vol. 245, pp. 496- 501 ,(1970) , 10.1016/S0021-9258(18)63360-5
Boanerges Rubalcava, Martin Rodbell, The Role of Acidic Phospholipids in Glucagon Action on Rat Liver Adenylate Cyclase Journal of Biological Chemistry. ,vol. 248, pp. 3831- 3837 ,(1973) , 10.1016/S0021-9258(19)43809-X
Michael C. Lin, David E. Wright, Victor J. Hruby, Martin Rodbell, Structure-function relations in glucagon. Properties of highly purified Des-his1-, monoiodo-, and [Des-Asn28,Thr29](homoserine lactone27)-glucagon Biochemistry. ,vol. 14, pp. 1559- 1563 ,(1975) , 10.1021/BI00679A002
A. C. Trakatellis, Kozue Tada, K. Yamaji, P. Gardiki-Kouidou, Isolation and partial characterization of anglerfish proglucagon Biochemistry. ,vol. 14, pp. 1508- 1512 ,(1975) , 10.1021/BI00678A025
H Sasaki, B Rubalcava, D Baetens, E Blazquez, C B Srikant, L Orci, R H Unger, Identification of glucagon in the gastrointestinal tract. Journal of Clinical Investigation. ,vol. 56, pp. 135- 145 ,(1975) , 10.1172/JCI108062
D. Baetens, IDENTIFICATION OF GLUCAGON-PRODUCING CELLS (A CELLS) IN DOG GASTRIC MUCOSA Journal of Cell Biology. ,vol. 69, pp. 455- 464 ,(1976) , 10.1083/JCB.69.2.455
H. S. Tager, D. F. Steiner, Isolation of a Glucagon-containing Peptide: Primary Structure of a Possible Fragment of Proglucagon Proceedings of the National Academy of Sciences of the United States of America. ,vol. 70, pp. 2321- 2325 ,(1973) , 10.1073/PNAS.70.8.2321
B. Noe, G. Bauer, M. Steffes, D. E. Sutherland, J. Najarian, Glucagon biosynthesis in human pancreatic islets: preliminary evidence for a biosynthetic intermediate. Hormone and Metabolic Research. ,vol. 7, pp. 314- 322 ,(1975) , 10.1055/S-0028-1093721