PROPERTIES OF ACHETAKININ BINDING-SITES ON MALPIGHIAN TUBULE MEMBRANES FROM THE HOUSE CRICKET, ACHETA-DOMESTICUS

被引：12
|
作者：
CHUNG, JS [1 ]
WHEELER, CH [1 ]
GOLDSWORTHY, GJ [1 ]
COAST, GM [1 ]
机构：
[1] UNIV LONDON BIRKBECK COLL,DEPT BIOL,LONDON WC1E 7HX,ENGLAND
来源：
PEPTIDES | 1995年 / 16卷 / 03期
关键词：
INSECT MYOKININS; ACHETAKININS; MALPIGHIAN TUBULES; RECEPTOR BINDING; DIURETIC PEPTIDES; ACHETA DOMESTICUS;
D O I：
10.1016/0196-9781(94)00207-M
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：
A biologically active I-125-labeled analogue of AK-II (3'-hydroxyphenyl propionic-Gly-Gly-Gly-Phe-Ser-Pro-Trp-Gly-NH2) was used to investigate the properties of achetakinin binding sites on plasma membranes from Malpighian tubules of Acheta domesticus. With optimized conditions, binding was rapid, reversible, and specific, and saturation studies revealed a single class of binding sites with K-d 0.55 nM and B-max 39.9 fmol/mg membrane protein. The affinities of achetakinins for binding sites on tubule membranes ranked AK-V > AK III > AK-II > AK-I greater than or equal to AK-IV, in general agreement with their potencies in functional assays. However, IC50 values were several orders of magnitude higher than corresponding values for EC(50) which suggests a considerable receptor reserve.
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页码：375 / 382
页数：8
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