CA2+-RESPONSIVE EXTENSIBLE MONOLAYER MEMBRANE OF CALMODULIN ALBUMIN CONJUGATE

被引：7

作者：

MIWA, T ^{[1
]}

KOBATAKE, E ^{[1
]}

IKARIYAMA, Y ^{[1
]}

AIZAWA, M ^{[1
]}

机构：

[1] TOKYO INST TECHNOL,FAC BIOSCI & BIOTECHNOL,DEPT BIOENGN,4259 NAGATSUTA,MIDORI KU,YOKOHAMA,KANAGAWA 227,JAPAN

来源：

BIOCONJUGATE CHEMISTRY | 1991年 / 2卷 / 04期

关键词：

SCANNING TUNNELING MICROSCOPY; CENTRAL HELIX; HYDROPATHIC CHARACTER; ENZYME ACTIVATION; PEPTIDE BINDING; ACIDIC PROTEIN; TARGET ENZYMES; BOVINE BRAIN; DELETIONS; FILMS;

D O I：

10.1021/bc00010a011

中图分类号：

Q5 [生物化学];

学科分类号：

071010 ; 081704 ;

摘要：

A Ca2+-responsive monolayer protein membrane was prepared by developing calmodulin and bovine serum albumin at the air-water interface and by conjugating them with a bifunctional agent. In the case of the BSA monolayer, complex formation with Mg2+ generated a larger change in surface pressure than that with Ca2+. On the other hand, a drastic change in surface pressure was observed for the conjugated thin membrane associated with Ca2+ than that associated with Mg2+. Due to a drastic change in the conformation of calmodulin, the conjugated protein film changes its morphology, (STM image), depending on Ca2+ concentration: the extended structure in the presence of Ca2+ transforms to a shrinked structure in the absence of Ca2+. The largest surface pressure change was detected when calmodulin was mixed with an equimolar amount of bovine serum albumin.

引用

页码：270 / 274

页数：5

共 24 条

[1] STRUCTURE OF CALMODULIN REFINED AT 2.2 A RESOLUTION [J].