SUPERACTIVE INSULINS

被引：24

作者：

BURKE, GT ^{[1
]}

HU, SQ ^{[1
]}

OHTA, N ^{[1
]}

SCHWARTZ, GP ^{[1
]}

ZONG, L ^{[1
]}

KATSOYANNIS, PG ^{[1
]}

机构：

[1] CUNY MT SINAI SCH MED,DEPT BIOCHEM,NEW YORK,NY 10029

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 1990年 / 173卷 / 03期

关键词：

D O I：

10.1016/S0006-291X(05)80882-4

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：

The substitution of aspartic acid for the naturally-occurring histidine residue in position B10 in human insulin results in an insulin analogue which displays an in vitro potency 4- to 5-fold greater than the parent compound. This substitution has been introduced into six insulin analogues which, before modification, display potencies ranging from less than 0.01-fold to 3-fold relative to natural insulin. In each case, the resulting aspartic acid-substituted analogue is substantially more potent than the parent compound. Thus, it is now possible to prepare "tailor-made" insulins with enhanced potency. © 1990 Academic Press, Inc.

引用

页码：982 / 987

页数：6

共 18 条

[1]

BARANY G, 1980, PEPTIDES ANAL SYNTHE, V2, P1

[2]

Blundell T.L., 1972, ADV PROTEIN CHEM, V26, P279

[3] DIVERGENCE OF THE INVITRO BIOLOGICAL-ACTIVITY AND RECEPTOR-BINDING AFFINITY OF A SYNTHETIC INSULIN ANALOG, [21-ASPARAGINAMIDE-A]INSULIN [J].