Literature DB >> 7066333

Partial characterization of bovine salivary proteins by electrophoretic methods.

W T Jones, R B Broadhurst, M P Gurnsey.   

Abstract

Electrophoresis in 71/2% polyacrylamide gel separates bovine salivary proteins into 12 bands, and is used as the first step, followed by isoelectrofocusing or electrophoresis in polyacrylamide (15%) gels containing sodium dodecyl sulphate (SDS) or immunoelectrophoresis in two-dimensional separations. Molecular weights of native proteins are determined by electrophoresis on gels of polyacrylamide concentration 10 to 20%. Using these methods, information on native and subunit molecular weights, isoelectric pH values and immunological relationships for bovine salivary proteins has been determined. Enzymic functions for six of the proteins were established by histological methods.

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Year:  1982        PMID: 7066333     DOI: 10.1016/0167-4838(82)90241-2

Source DB:  PubMed          Journal:  Biochim Biophys Acta        ISSN: 0006-3002


  2 in total

1.  Molecular cloning of a cDNA encoding aspartate aminotransferase-P2 from lupin root nodules.

Authors:  P H Reynolds; L A Smith; J M Dickson; W T Jones; S D Jones; K A Rodber; A Carne; C P Liddane
Journal:  Plant Mol Biol       Date:  1992-06       Impact factor: 4.076

2.  Production and Characterization of Monoclonal Antibodies against Aspartate Aminotransferase-P1 from Lupin Root Nodules.

Authors:  W. T. Jones; S. D. Jones; D. Harvey; K. R. Rodber; G. B. Ryan; PHS. Reynolds
Journal:  Plant Physiol       Date:  1994-01       Impact factor: 8.340

  2 in total

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