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Primary structure of a lambda Bence Jones protein (Os).
Bull Osaka Med Coll. 1989 Nov; 35(1-2):61-70.BO

Abstract

The primary structure of a human lambda type Bence-Jones protein Os was determined by analyzing amino acid sequence of the completely reduced and aminoethylated protein. Nineteen tryptic peptides covering 213 residues were isolated and 10 of these were completely sequenced. For the remaining peptides, only partial sequences or the amino acid composition were determined. All the tryptic peptides could be arranged in order on the basis of the above results and homology with other lambda chains of known sequences. The sequence of the variable region, which contains 109 residues, is homologous with those of proteins of subgroup V lambda I. The sequence of the constant region indicates that protein Os has Mcg(+), Kern(+) and Oz(-) as isotypic markers, in spite of having a unique residue at position 164.

Authors+Show Affiliations

Department of Legal Medicine, Osaka Medical College, Japan.No affiliation info available

Pub Type(s)

Journal Article

Language

eng

PubMed ID

2486244

Citation

Ito, S, and H Matsumoto. "Primary Structure of a Lambda Bence Jones Protein (Os)." Bulletin of the Osaka Medical College, vol. 35, no. 1-2, 1989, pp. 61-70.
Ito S, Matsumoto H. Primary structure of a lambda Bence Jones protein (Os). Bull Osaka Med Coll. 1989;35(1-2):61-70.
Ito, S., & Matsumoto, H. (1989). Primary structure of a lambda Bence Jones protein (Os). Bulletin of the Osaka Medical College, 35(1-2), 61-70.
Ito S, Matsumoto H. Primary Structure of a Lambda Bence Jones Protein (Os). Bull Osaka Med Coll. 1989;35(1-2):61-70. PubMed PMID: 2486244.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Primary structure of a lambda Bence Jones protein (Os). AU - Ito,S, AU - Matsumoto,H, PY - 1989/11/1/pubmed PY - 1989/11/1/medline PY - 1989/11/1/entrez SP - 61 EP - 70 JF - Bulletin of the Osaka Medical College JO - Bull Osaka Med Coll VL - 35 IS - 1-2 N2 - The primary structure of a human lambda type Bence-Jones protein Os was determined by analyzing amino acid sequence of the completely reduced and aminoethylated protein. Nineteen tryptic peptides covering 213 residues were isolated and 10 of these were completely sequenced. For the remaining peptides, only partial sequences or the amino acid composition were determined. All the tryptic peptides could be arranged in order on the basis of the above results and homology with other lambda chains of known sequences. The sequence of the variable region, which contains 109 residues, is homologous with those of proteins of subgroup V lambda I. The sequence of the constant region indicates that protein Os has Mcg(+), Kern(+) and Oz(-) as isotypic markers, in spite of having a unique residue at position 164. SN - 0916-2844 UR - https://www.unboundmedicine.com/medline/citation/2486244/Primary_structure_of_a_lambda_Bence_Jones_protein__Os__ DB - PRIME DP - Unbound Medicine ER -