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Fractionation of parotid salivary proteins by isoelectric focusing in a wide pH range
Author(s) -
ARNEBERG PÅL
Publication year - 1972
Publication title -
european journal of oral sciences
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.802
H-Index - 93
eISSN - 1600-0722
pISSN - 0909-8836
DOI - 10.1111/j.1600-0722.1972.tb00273.x
Subject(s) - isoelectric focusing , chromatography , chemistry , lysozyme , fractionation , isoelectric point , sephadex , immobilized ph gradient , electrophoresis , size exclusion chromatography , saliva , amylase , biochemistry , enzyme
– Human parotid saliva was fractionated on an isoelectric focusing column (LKB 8102, ampholyte pH 3–10). Each fraction was run through a Sephadex® G‐50 column to remove sucrose and carrier ampholytes. Amylase focused at pH 6‐7 and lysozyme at pH about 11. Other protein components were found at pH 4–5, at pH about 9 and above 10. The two peaks at alkaline pH comprised glycoproteins. Analytical disc electrophoresis revealed that each of the peaks contained several protein species. Isoelectric focusing as described has a capacity of about 200 mg of parotid salivary protein and is well suited as an initial fractionation step. However, the steep pH gradient used does not allow the separation of proteins with close pI and some small proteins are probably lost in the subsequent gel filtration.