Biochemical properties of tissue polypeptide antigen.
作者： B. Lüning , B. Wiklund , P. Redelius , B. Björklund
DOI: 10.1016/0005-2795(80)90228-7
关键词: Chemistry 、 Leucine 、 Isoelectric focusing 、 Amino acid 、 Isoelectric point 、 Molecular biology 、 Antigen 、 Protein subunit 、 Tissue Polypeptide Antigen 、 Aspartic acid 、 Biochemistry
摘要: Tissue polypeptide antigen (TPA) is a complex protein which has been originally identified in extracts of pooled tumors using horse antisera raised against the insolubles human tumor cells. The now routinely detected and measured by previously described hemagglutination inhibition assay. It shown this method that concentration higher tissues sera cancer patients as compared to normal or sera, respectively. In aqueous solutions, pH 2-12, TPA tendency form high molecular weight aggregates. However they can be dissociated sodium dodecyl sulfate into subunits, each appearing single chain peptide: B1 (Mr 4.3 x 10(4)), B2 3.0 C 1.7 10(4)). subunits saturate anti-TPA serum indistinguishably from TPA. Amino acid composition dominated glutamic acid, aspartic leucine, cysteine being absent subunit B1. isoelectric point main subunit, B1, 4.4-4.6. Sedimentation diffusion analyses indicate pure solution exists distinct oligomeric states.
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