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- W2017806507 abstract "Abstract Amylase was isolated from human submandibular-sublingual saliva by BioGel P-2 filtration, ammonium sulphate precipitation and DEAE-Sephadex chromatography. The purified enzyme was separated into isoenzyme families A and B on Bio-Gel P-100 and the families were compared with the corresponding families of human parotid amylase. The respective enzymes exhibited identical specific enzymatic activities and isoenzyme patterns on polyacrylamide disc gels. Family A of human submandibular amylase contained the equivalent of 6 moles of covalently linked neutral sugar per mole of enzyme as compared to 7 moles/mole for the parotid family A. Family B contained no carbohydrate. The proportion of submandibular amylase that is glycosylated (25 per cent) is the same as in the parotid. All α-amylases tested exhibited an unusual absorption spectrum with a maximum at 405 nm when reacted with the phenol-sulphuric acid reagent. The A families of both human parotid and submandibular amylases have an additional maximum at 485 nm, typical of glycoproteins. The B families do not exhibit the second maximum." @default.
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- W2017806507 date "1973-09-01" @default.
- W2017806507 modified "2023-09-25" @default.
- W2017806507 title "The existence of glycosylated and non-glycosylated forms of human submandibular amylase" @default.
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- W2017806507 doi "https://doi.org/10.1016/0003-9969(73)90084-8" @default.
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