Work

Bovine Erythrocyte Superoxide Dismutase

Year: 1974

Type: article

Abstract: The complete primary structure of reduced and S-carboxy-methylated bovine erythrocyte superoxide dismutase has been derived through analysis of peptides from peptic, plasmin, and hydroxylamine digests of the intact polypeptide chain, and from chymotryptic, subtilisin, and dilute acid digests of derived peptides. From these data, the following unique amino acid sequence of 151 residues was deduced, corresponding to a molecular weight of 15,600, in each of the 2 apparently identical subunits of the protein molecule. (Cmc denotes S-carboxymethylcysteine.) [see PDF for equation]

Source: Journal of Biological Chemistry

DOI: 10.1016/s0021-9258(19)42108-x

Authors: Howard M. Steinman, Vishweshwar R. Naik, John L. Abernethy, Robert L. Hill

Institution: Duke Medical Center

Language: English

Topic: Enzyme Structure and Function

Subfield: Materials Chemistry

Field: Materials Science

Domain: Physical Sciences

Open Access status: hybrid

Estimated APC paid: $3,430

OpenAlex ID: W1898798642

FWCI: 14.15

Cites: 55

Cited by: 224

Related to: 10