Partial characterization of bovine salivary proteins by electrophoretic methods

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...

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Bibliographic Details
Published inBiochimica et biophysica acta Vol. 701; no. 3; pp. 382 - 388
Main Authors Jones, W.T, Broadhurst, R.B, Gurnsey, M.P
Format Journal Article
LanguageEnglish
Published Netherlands 01.01.1982
Subjects
animal physiology
Animals
Cattle
Electrophoresis, Polyacrylamide Gel
Immunoelectrophoresis, Two-Dimensional
Isoelectric Focusing
Mercaptoethanol - pharmacology
Molecular Weight
Oxidation-Reduction
Salivary Proteins and Peptides - isolation & purification
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Summary: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.
Bibliography:ObjectType-Article-1
SourceType-Scholarly Journals-1
ObjectType-Feature-2
content type line 23
ISSN:0006-3002
1878-2434
DOI:10.1016/0167-4838(82)90241-2