[Significance of urinary alanine aminopeptidase analysis in clinical tests].
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Biomedical subjects
Publications and source records attributed to M Yakata.
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Wheat germ lectin affinity electrophoresis was employed for quantitating the bone and liver isoenzymes of alkaline phosphatase (EC 3.1.3.1) in serum and for determining the reference limits of each isoenzyme activity in 488 healthy individuals. Bone phosphatase activity was detected even after bone growth, accounting for 60-70% of the total activity. An increase in bone phosphatase activity occurred in older females, but there was a decrease in older males. Liver phosphatase activity gradually increased with age in both sexes, males showing higher activity than females at all ages. Wheat germ lectin affinity electrophoresis of serum alkaline phosphatase is a simple and useful method for quantitating bone and liver alkaline phosphatase activities.
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A slow albumin variant was isolated from the serum of a patient with bisalbuminemia. Reverse-phase peptide mapping revealed a single altered peak when tryptic digests of the normal and variant albumin were compared. After rechromatography and amino acid analysis, a sequence of Tyr-Ile-Cys-Glu-Asn-Gln-Gly-Ser was obtained for the mutant peptide, while a sequence of Tyr-Ile-Cys-Glu-Asn-Gln-Asp-Ser was obtained for the normal peptide. This establishes the mutation as 269 Asp----Gly and the new albumin has been named albumin Niigata.
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