Amino acid sequence of the sulfate-binding protein from Salmonella typhimurium LT2

The amino acid sequence of the sulfate-binding protein from Salmonella typhimurium LT2 was determined by automated sequenator analysis of whole protein and fragments derived by chemical and enzymatic cleavage of whole protein. The fragments were products of limited trypsin digestion at arginine, cle...

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Bibliographic Details
Published in:The Journal of biological chemistry 1980-05, Vol.255 (10), p.4614-4618
Main Authors: Isihara, H, Hogg, R W
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Carrier Proteins
Chymotrypsin
Hydroxylamines
Peptide Fragments - analysis
Peptide Hydrolases
Salmonella typhimurium - metabolism
Sulfates
Trypsin
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Summary:The amino acid sequence of the sulfate-binding protein from Salmonella typhimurium LT2 was determined by automated sequenator analysis of whole protein and fragments derived by chemical and enzymatic cleavage of whole protein. The fragments were products of limited trypsin digestion at arginine, cleavage at tryptophan by BrNps-skatole and o-iodosobenzoic acid, digestion with the protease from Staphylococcus aureus V8 at Glu-X bonds, cleavage by hydroxylamine at Asn-Gly bonds, and subdigestion with trypsin, chymotrypsin, and the Staphylococcus protease. The COOH-terminal sequence was confirmed using carboxypeptidase B and amino acid analysis. The sulfate-binding protein was determined to contain a single polypeptide of 310 residues with a molecular weight of 34,667 calculated from the sequence.
ISSN:0021-9258
1083-351X
DOI:10.1016/S0021-9258(19)85539-4