These tools will no longer be maintained as of December 31, 2024. Archived website can be found here. PubMed4Hh GitHub repository can be found here. Contact NLM Customer Service if you have questions.


Pubmed for Handhelds

PUBMED FOR HANDHELDS

Search MEDLINE/PubMed

  • Title: Reinvestigation of extremely acidic proteins in bovine brain.
    Author: Isobe T, Nakajima T, Okuyama T.
    Journal: Biochim Biophys Acta; 1977 Sep 27; 494(1):222-32. PubMed ID: 901807.
    Abstract:
    Analysis of bovine brain extract by disc electrophoresis on a 20% polyacrylamide gel indicated the existence of three extremely acidic proteins. These proteins were isolated by column chromatography on DEAE-Sephadex A-50 and Sephadex G-75. The isolated proteins (PAP I-a, PAP I-b and PAP II) were homogeneous in various methods including 7.5% and 20% gel electrophoresis or gel chromatography, and share, in the extract, 85% of the total of the acidic proteins that migrate with the bromophenol blue marker in 7.5% gels. Their physicochemical properties, including molecular weight, ultraviolet absorption spectra or amino acid composition were similar, especially those between PAP I-a and PAP I-b where a part of primary structure appeared to be common in their tryptic peptide maps. These two proteins were identified to be the nervous system specific protein S 100 by immunochemical and electrophoresis methods as well as by amino acid analysis, and the other protein PAP II was revealed to be a calcium-binding protein. The existence and properties of the isolated proteins are discussed with relation to the heterogeneity problem of S 100 protein.
    [Abstract] [Full Text] [Related] [New Search]