✦ LIBER ✦

Electrophoretic characterisation of human parotid saliva protein fractions isolated by preparative isoelectric focusing

✍ Scribed by Dr. Frank M. Hallinan; Marie Rose; Marie Eagleton; Edward Tempany

Publisher: John Wiley and Sons
Year: 1986
Tongue: English
Weight: 858 KB
Volume: 7
Category: Article
ISSN: 0173-0835
DOI: 10.1002/elps.1150070709

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✦ Synopsis

Electrophoretic characterisation of human parotid saliva protein fractions isolated by preparative isoelectric focusing Children's Research Centre, Dublin

Human parotid saliva proteins fractionated by preparative isoelectric focusing into 3 main fractions have been characterised electrophoretically and immunochemically.

The anodic proteins constitute a polymorphic family of collagenase and trypsin sensitive, immunochemically related, phosphoproteins. Many of these contain a common polypeptide of M, 23 000 either alone or in combination with other lower (MI 21 000) or higher (Mr 25 000) molecular weight polypeptides. Parotid amylase was substantially purified by this technique and an antiserum against these fractions reacted monospecifically with amylase in a number of systems. The cathodic proteins are all collagenase sensitive proteins with M, values of 12 500 to 77 000.

Materials and methods

2.1 Chemicals

The following reagents were obtained from the sources indicated: Ampholines and Ultrodex

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