1973
DOI: 10.1007/bf00485989
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Evidence for post-transcriptional modification of human salivary amylase (Amy1) isozymes

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Cited by 47 publications
(11 citation statements)
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“…Heterogeneity of a-amylase isozymes in human salivary gland and pancreas is considered to result from posttranslational modification, e.g. glycosylation and deamidation (13). To elucidate the origin of heterogeneity of rice a-amylase isozymes, the inhibition of glycosylation by TM in combination with in vitro translation has been determined.…”
mentioning
confidence: 99%
“…Heterogeneity of a-amylase isozymes in human salivary gland and pancreas is considered to result from posttranslational modification, e.g. glycosylation and deamidation (13). To elucidate the origin of heterogeneity of rice a-amylase isozymes, the inhibition of glycosylation by TM in combination with in vitro translation has been determined.…”
mentioning
confidence: 99%
“…As a result of isozyme identification, however, the female genital tract was implicated since the elevated amylase was shown to be of the salivary type [28]. Clinical amylase determinations are complemented by techniques which allow the identification of the source of the elevated isozyme(s) [reviewed in 2], Over the past 15 years several investigators have reported rapidly migrating amylase isozymes in nor mal genital tract tissue [27] and in the sera and urines of women with tumors of the reproductive tract [1, 17.…”
Section: Discussionmentioning
confidence: 99%
“…A second case involves the interesting situation of the salivary amylases (AMYL) reported by Karn et al (1973). However, the enzyme catalyzing this process is produced not by another locus in the human genome, but rather by the bacterial flora in the mouth.…”
Section: Stability Variantsmentioning
confidence: 99%