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Identification and isolation of actin from Neurospora crassa.

Authors
  • Sikora, L
  • Marzluf, G A
Type
Published Article
Journal
Journal of General Microbiology
Publisher
Microbiology Society
Publication Date
Mar 01, 1982
Volume
128
Issue
3
Pages
439–445
Identifiers
PMID: 6281363
Source
Medline
License
Unknown

Abstract

Crude cell extracts of Neurospora crassa contained 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. The N. crassa actin was purified by DEAE-cellulose and DNAase I-Sepharose chromatography and had the expected property of inhibiting DNAase I activity. Although N. crassa actin 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.

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