Identification and isolation of actin from Neurospora crassa.
Identification and isolation of actin from Neurospora crassa.
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粗糙脉孢菌肌动蛋白的鉴定和分离。
DOI：
10.1099/00221287-128-3-439
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发表时间：
1982
期刊：
影响因子：
--
通讯作者：
Marzluf,GA
中科院分区：
文献类型：
--
作者：
Sikora,L;Marzluf,GA
粗糙脉孢菌的粗细胞提取物含有丰富的蛋白质，通过多种标准将其鉴定为肌动蛋白。该蛋白质，无论是细胞提取物还是纯形式，都与聚丙烯酰胺凝胶中的兔骨骼肌肌动蛋白共同迁移。然后。 crassaactin 通过 DEAE-纤维素和 DNAase I-Sepharose 层析纯化，具有抑制 DNAase I 活性的预期特性。虽然N. crassaactin可以聚合和解聚，完全根据这个特性进行纯化是无效的。肌动蛋白容易被蛋白水解降解，并且在某些条件下，观察到特定大小的分解产物。
Crude cell extracts ofNeurospora crassacontained an abundant protein that was identified as actin by a number of criteria. The protein, either in cell extracts or in pure form, co-migrated with rabbit skeletal muscle actin in polyacrylamide gels. TheN. crassaactin was purified by DEAE-cellulose and DNAase I-Sepharose chromatography and had the expected property of inhibiting DNAase I activity. AlthoughN. crassaactin could polymerize and depolymerize, purification based entirely on this characteristic was ineffective. The actin was susceptible to proteolytic degradation, and under certain conditions, a breakdown product of defined size was observed.