Topic
Amylase
About: Amylase is a research topic. Over the lifetime, 14164 publications have been published within this topic receiving 296069 citations.
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TL;DR: The present results confirm that endocrine-acinar cells do appear within the islets of Langerhans as well as in the acinar parenchyma and may represent intermediate steps in a transdifferentiating process.
Abstract: When tissues were subjected to 24 h of duct ligation, intermediate pancreatic cells simultaneously displaying endocrine and exocrine phenotypes appeared. Immunocytochemistry by laser scanning confocal microscopy revealed the appearance of a large number of these cells coexpressing insulin and amylase. These cells were located within the islets of Langerhans as well as in the acinar parenchyma. They were also detected in a culture system of isolated pancreatic cells. With the use of immunoelectron microscopy, two types of secretory granules were identified in these cells. One was insulin immunoreactive, whereas the other, resembling zymogen granules, contained amylase. Occasionally, some small granules displayed a double labeling for both secretory proteins. Numerous crinophagic bodies and autophagosomes containing insulin and/or amylase were also present. In situ hybridization, applied with the specific probes, confirmed the presence of both insulin and amylase mRNAs in these cells. Because duct ligation is known to induce insulin cell proliferation, the present results confirm that endocrine-acinar cells do appear in such condition and may represent intermediate steps in a transdifferentiating process.
74 citations
TL;DR: In this article, a yeast strain YF207/pGA11/pAA12 co-displaying Glucoamylase and Bacillus stearothermophilus α amylase was used to produce ethanol from low-temperature-cooked corn starch.
74 citations
TL;DR: In this article, the ability of fresh tropical fruits to inhibit starch-hydrolyzing enzymes was determined by using high-performance liquid chromatography coupled with diode array detector.
74 citations
TL;DR: This study designs and synthesizes thiadiazole quinoline analogs (1-30), characterized by different spectroscopic techniques such as 1HNMR and EI-MS and identifies novel series of potent α-amylase inhibitors for further investigation.
74 citations
TL;DR: An α‐amylase gene from Bacillus sp.
Abstract: An alpha-amylase gene from Bacillus sp. strain TS-23 was cloned and expressed by using its own promoter on the recombinant plasmid pTS917 in Escherichia coli. A cell fractionation experiment revealed that approximately 60% of the amylase activity was in the periplasmic space. Analysis and activity staining of the concentrated supernatant fraction by SDS-polyacrylamide gel electrophoresis showed an apparent protein band with a mol. wt of approximately 65,000. The amylase gene (amyA) consisted of an open reading frame of 1,845 bp encoding a protein of 613 amino acids with a calculated mol. wt of 69,543. The predicted amino acid sequence showed high homology with Bacillus species, E. coli and Salmonella typhimurium alpha-amylases. Deletion of 96 amino acids from the C-terminal portion of the amylase did not result in the loss of amylolytic activity. The truncated amylase, deletion of the first 50 amino acids from the N-terminus, was overexpressed in E. coli system and refolded to yield an activable enzyme.
74 citations