PURIFICATION AND CHARACTERIZATION OF THE PARVALBUMIN FROM MONKEY SKELETAL-MUSCLE

被引：5

作者：

ASAOKA, K ^{[1
]}

TANOKURA, M ^{[1
]}

机构：

[1] MED COLL OITA,DEPT PHYSIOL,OITA 87956,JAPAN

来源：

COMPARATIVE BIOCHEMISTRY AND PHYSIOLOGY B-BIOCHEMISTRY & MOLECULAR BIOLOGY | 1990年 / 96卷 / 04期

关键词：

D O I：

10.1016/0305-0491(90)90211-B

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：

1. 1. A high affinity Ca2+ binding and low mol. wt protein, parvalbumin, was purified from monkey skeletal muscle. 2. 2. As compared with other animals, only one component and a lower content of monkey parvalbumin were found. 3. 3. This may suggest that both the component and the content of parvalbumin decreases with biological evolution. 4. 4. The parvalbumin was found to have a mol. wt of 11,400, a pI of 5.1, a high aspartic acid and lysine content, maximum absorption at around 260nm, a blocked amino-terminal, an immunological distinction, 2 mol Ca2+ binding/mol, and a conformational change by Ca2+ binding. 5. 5. Parvalbumin was shown to have alpha type properties. © 1990.

引用

页码：665 / 669

页数：5

共 22 条

[1] ESTIMATION OF MOLECULAR WEIGHTS OF PROTEINS BY SEPHADEX GEL-FILTRATION [J].