The primary structure of actin from rabbit skeletal muscle. Five cyanogen bromide peptides, including the NH2 and COOH termini.
Open Access
- 1 August 1975
- journal article
- abstracts
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 250 (15) , 5897-5905
- https://doi.org/10.1016/s0021-9258(19)41137-x
Abstract
No abstract availableKeywords
This publication has 28 references indexed in Scilit:
- Solid‐phase edman degradation: Attachment of carboxyl‐terminal homoserine peptides to an insoluble resinFEBS Letters, 1973
- Solid‐phase Edman degradation. The use of p‐phenyl diisothiocyanate to attach lysine‐ and arginine‐containing peptides to insoluble resinsFEBS Letters, 1972
- Amino acid sequence around the single 3-methylhistidine residue in rabbit skeletal muscle myosinBiochemistry, 1971
- Amino acid sequence around 3-methylhistidine in rabbit skeletal muscle actinBiochemistry, 1971
- Spin-labeled actinBiochemistry, 1970
- Structural studies on rabbit skeletal actin. I. Isolation and characterization of the peptides produced by cyanogen bromide cleavageBiochemistry, 1970
- Amino acid sequence studies on rabbit skeletal muscle actin. Cyanogen bromide cleavage of the protein and determination of the sequences of seven of the resulting peptidesBiochemistry, 1970
- Characterization of sulfhydryl groups of actinBiochemistry, 1969
- The sulfhydryl groups of actinArchives of Biochemistry and Biophysics, 1968
- Studies on actin-actin and actin-myosin interactionBiochimica et Biophysica Acta (BBA) - Protein Structure, 1967