Thymosin alpha1: isolation and sequence analysis of an immunologically active thymic polypeptide.
Author(s) -
Adam Lee Goldstein,
Teresa L. K. Low,
Martha H. McAdoo,
John E. McClure,
Gary B. Thurman,
Jeffrey L. Rossio,
C.Y. Lai,
David Chang,
S S Wang,
Clifford L. Harvey,
A. Ramel,
Johannes Meienhofer
Publication year - 1977
Publication title -
proceedings of the national academy of sciences
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.011
H-Index - 771
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.74.2.725
Subject(s) - thymosin , peptide sequence , peptide , biochemistry , biology , amino acid , sequence (biology) , protein primary structure , microbiology and biotechnology , chemistry , gene
The amino acid sequence of a biologically active polypeptide isolated from calf thymus, termed thymosin alpha1, has been determined. Thymosin alpha1 is a heat stable, highly acidic molecule composed of 28 amino acid residues. This peptide is one of several present in thymosin fraction 5 that may participate in the regulation, differentiation and function of thymus-dependent lymphocytes (T cells). A nomenclature for the family of polypeptides present in thymosin fraction 5 is suggested.
Accelerating Research
Robert Robinson Avenue,
Oxford Science Park, Oxford
OX4 4GP, United Kingdom
Address
John Eccles HouseRobert Robinson Avenue,
Oxford Science Park, Oxford
OX4 4GP, United Kingdom