CYCLIC-AMP-DEPENDENT PHOSPHORYLATION OF GLICENTIN

被引：7

作者：

CONLON, JM

THIM, L

MOODY, AJ

SOLING, HD

机构：

[1] NOVO RES INST, COPENHAGEN, DENMARK

[2] UNIV GOTTINGEN, ZENTRUM INNERE MED, KLIN BIOCHEM ABT, D-3400 GOTTINGEN, FED REP GER

来源：

BIOSCIENCE REPORTS | 1984年 / 4卷 / 06期

关键词：

D O I：

10.1007/BF01122224

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Highly purified glicentin, a 69-amino-acid-residue peptide isolated from porcine intestine that contains the full sequence of glucagon and is probably biosynthetically related to glucagon, is a substrate for cAMP-dependent protein kinase in a cell-free system. Glicentin-related pancreatic peptide (residues 1-30 of glicentin) and glucagon were not phosphorylated under the same conditions. The serine residue at position 34 of glicentin (position 2 of glucagon), that is part of the sequence Lys-Arg-His-Ser, is the probable site of phosphorylation.

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页码：489 / 496

页数：8

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