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Human salivary alpha‐amylase Purification and amino acid composition
Author(s) -
HENSTENFETTERSEN ARNE,
SØNJU TORLEIF,
BEST TONE
Publication year - 1970
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.1600-0722.1970.tb02095.x
Subject(s) - amylase , saliva , chromatography , chemistry , alpha amylase , isoamylase , alpha (finance) , electrophoresis , parotid gland , biochemistry , acetone , enzyme , dentistry , medicine , construct validity , nursing , patient satisfaction
— Human salivary alpha‐amylase was purified by ammonium sulfate‐acetone precipitations, and residual impurities removed by adsorption chromatography on hydroxylapatite columns. Subsequent preparative disc electrophoresis indicated that parotid alpha‐amylase from one person was a single moiety, whereas alpha‐amylase from pooled, whole saliva was separated into two components. One of these had the same electrophoretic mobility as the parotid alpha‐amylase. The amino acid compositions of these components were determined and compared with monkey and rabbit parotid alpha‐amylase and with the results of an earlier investigation of human alpha‐amylase from pooled, whole saliva. Significant differences were not observed.