CRITICAL-EVALUATION OF A THEORY OF MOLECULAR RECOGNITION USING HUMAN INSULIN-LIKE-GROWTH-FACTOR-I FRAGMENT 21-40 AND ITS COMPLEMENTARY PEPTIDE

被引:12
作者
BEATTIE, J
FLINT, DJ
机构
[1] Hannah Research Institute
关键词
D O I
10.1042/bj2830473
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
Using solid-phase methods we have synthesized human insulin-like-growth-factor-I (IGF-I) fragment 21-40 (IGF-I 21-40) and the peptide derived from the 5' --> 3' translation of the complementary nucleic acid of this peptide, 'I-FGI 20-40' (the complementary peptide). According to a recently proposed theory of molecular recognition, these two peptides should bind specifically to each other. We have tested this theory by using both solid- and solution-phase direct-binding assays for this complementary-peptide pair. We have also investigated the ability of I-FGI 20-40 to interfere with native IGF-I binding during radioimmunoassay (r.i.a.), radio-receptor (r.r.a.), assay and ligand-blot analysis of IGF- binding proteins. We have obtained no evidence of any interaction between IGF-I 20-40 and I-FGI 20-40 in either solid- or solution-phase assays. In addition, I-FGI 20-40 does not interfere in the assays used to detect IGF-I binding antibodies (r.i.a.), receptors (r.r.a.) or binding proteins (ligand blots). Our data therefore question the universality of this particular theory of molecular recognition.
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页码:473 / 478
页数:6
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