Literature DB >> 1112043

Comparison of human pancreatic and parotid amylase activities on different substrates.

D J Stiefel, P J Keller.   

Abstract

The specific activities of highly purified preparations of human parotid and pancreatic amylase on several different soluble and insoluble starches were compared. The ratio of parotid to pancreatic activity varied with the physical nature of the substrate. With all soluble starches, irrespective of source, parotid amylase exhibited a higher specific activity than did pancreatic amylase; the reverse was true for an insoluble chromogenic starch (Amylose Azure). The variation in enzyme-substrate interaction supports previous indications of configurational differences between the two amylases. The observed organ-specific characteristics according to organ of origin may have value in determining relative parotid and pancreatic amylase activities in body fluids under normal and pathological conditions, thereby helping to clarify their functional and clinical significance.

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Year:  1975        PMID: 1112043

Source DB:  PubMed          Journal:  Clin Chem        ISSN: 0009-9147            Impact factor:   8.327


  2 in total

1.  Substrate specificity for pancreatic amylase.

Authors:  T Takeuchi; T Kozu; S Watanabe; M Morita; K Shiratori; I Shibata
Journal:  Gastroenterol Jpn       Date:  1978

2.  Salivary α-amylase exhibits antiproliferative effects in primary cell cultures of rat mammary epithelial cells and human breast cancer cells.

Authors:  Maren Fedrowitz; Ralf Hass; Catharina Bertram; Wolfgang Löscher
Journal:  J Exp Clin Cancer Res       Date:  2011-10-25
  2 in total

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