PURIFICATION AND BIOCHEMICAL-CHARACTERIZATION OF CALMODULIN FROM CORYLUS-AVELLANA POLLEN

被引：0

作者：

SCALI, M

CAI, G

DELCASINO, C

SANTUCCI, A

TIRLAPUR, UK

MOSCATELLI, A

CRESTI, M

TIEZZI, A

机构：

[1] UNIV SIENA,DIPARTIMENTO BIOL MOLEC,I-53100 SIENA,ITALY

[2] UNIV TUSCIA,DIPARTIMENTO SCI AMBIENTALI,I-01100 VITERBO,ITALY

来源：

PLANT PHYSIOLOGY AND BIOCHEMISTRY | 1994年 / 32卷 / 06期

关键词：

D O I：

暂无

中图分类号：

Q94 [植物学];

学科分类号：

071001 ;

摘要：

A calcium-binding protein identifiable as calmodulin has been isolated from Corylus avellana L. pollen by phenyl-sepharose chromatography and further purified by anion exchange fast protein liquid chromatography. This protein is recognized by a monoclonal antibody raised against pea calmodulin. It can activate bovine brain phosphodiesterase in a calcium dependent manner and shows a calcium dependent shift in electrophoretic mobility. 2-D gel electrophoresis reveals that the polypeptide is present as a single isoform in Corylus pollen. In addition the amino acid sequence of this protein is largely comparable to that of other known plant calmodulins and to bovine brain calmodulin.

引用

页码：831 / 838

页数：8

共 30 条

[1]

BRADFORD MM, 1976, ANAL BIOCHEM, V72, P248, DOI 10.1016/0003-2697(76)90527-3

[2] INTERACTION OF CALCIUM AND CALMODULIN IN THE PRESENCE OF SODIUM DODECYL-SULFATE [J].