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The Annals of Otology, Rhinology, and... 1986Amylase, an enzyme that hydrolyzes starch, has been localized in the nasal mucosa for the first time by the protein A-gold technique. The amylase appeared to be produced...
Amylase, an enzyme that hydrolyzes starch, has been localized in the nasal mucosa for the first time by the protein A-gold technique. The amylase appeared to be produced by serous cells of the nasal glands. This enzyme has the potential for use as a tumor marker for cancer of the nasal cavity. The function of amylase in the physiology of nasal secretions is discussed.
Topics: Adult; Amylases; Histocytochemistry; Humans; Microscopy, Electron; Nasal Mucosa
PubMed: 2424357
DOI: 10.1177/000348948609500314 -
Lancet (London, England) Dec 1972
Topics: Amylases; Filtration; Humans; Kidney Glomerulus; Molecular Weight; Pancreas; Pancreatitis
PubMed: 4118215
DOI: No ID Found -
Journal of Industrial Microbiology &... Jul 2005Arthrobacter psychrolactophilus ATCC 700733 grew with a doubling time of 1.5-2.3 h (22 degrees C) and produced up to 0.2 units/mL (soluble starch assay) of extracellular...
Arthrobacter psychrolactophilus ATCC 700733 grew with a doubling time of 1.5-2.3 h (22 degrees C) and produced up to 0.2 units/mL (soluble starch assay) of extracellular amylase in tryptic soy broth without dextrose (TSBWD) containing 0.5% or 1.0% (w/v) soluble starch or maltose as the fermentable substrate. Time-course experiments in media containing soluble starch as substrate showed that amylolytic activity appeared in cultures at 24 h (after exponential growth had ceased), reached peak levels in 72-96 h, and declined rapidly after reaching peak levels. Peak levels were highest in TSBWD containing 1.0% soluble starch. Proteolytic activity appeared at about the same time as amylolytic activity and increased during the period of amylase production. Significant amylase production was not observed in cultures in TSBWD with 0.5% glucose or in cultures grown at 28 degrees C, but low levels of amylase were observed in TSBWD cultures grown at 19-23 degrees C which contained no added carbohydrate. A single band of activity was observed after electrophoresis of supernatant fractions in non-denaturing gels, followed by in situ staining for amylolytic activity. The amylase possessed a raw starch-binding domain and bound to uncooked corn, wheat or potato starch granules. It was active in the Phadebas assay for alpha-amylase. Activity was maximum on soluble starch at a temperature between 40 degrees C and 50 degrees C. The amylase after purification by affinity chromatography on raw starch granules exhibited two starch-binding protein bands on SDS gels of 105 kDa and 26 kDa.
Topics: Amylases; Arthrobacter; Bacterial Proteins; Enzyme Stability; Starch; Temperature; Time Factors
PubMed: 15931519
DOI: 10.1007/s10295-005-0240-3 -
Journal of Dairy Science Jun 1979Three amylase phenotypes, AmIB, AmIC, and AmIBC, were detected by electrophoresis of blood serum from 329 Holstein cattle. These phenotypes appear to be controlled by...
Three amylase phenotypes, AmIB, AmIC, and AmIBC, were detected by electrophoresis of blood serum from 329 Holstein cattle. These phenotypes appear to be controlled by two alleles AmIB and AmIC at the amylase I locus (AmI). Frequencies were .518 and .482 for alleles B and C. The numbers of phenotypes corresponded closely to expectations of Hardy-Weinberg equilibrium. No evidence of linkage between the AmI locus and other genetic marker loci of blood and milk was detected.
Topics: Amylases; Animals; Cattle; Genetic Linkage; Genetic Variation; Genotype
PubMed: 500897
DOI: 10.3168/jds.S0022-0302(79)83358-5 -
Forensic Science Dec 1975Amylase levels in body fluids are reported, and it is shown that high amylase levels may occasionally occur in body fluids other than saliva. Low amylase levels are...
Amylase levels in body fluids are reported, and it is shown that high amylase levels may occasionally occur in body fluids other than saliva. Low amylase levels are reported in a saliva component which has been previously described as being rich in blood group active material. The use of amylase activity in the localisation and identification of saliva is discussed in detail and guidelines for the interpretation of results are proposed.
Topics: Amylases; Body Fluids; Humans; Lip; Male; Saliva; Semen; Sweat; Tears
PubMed: 1225775
DOI: 10.1016/0300-9432(75)90004-7 -
The Biochemical Journal May 1962
Topics: Amylases; Bacillus subtilis; alpha-Amylases
PubMed: 13880470
DOI: 10.1042/bj0830256 -
FEMS Microbiology Letters Apr 1992The enzymatic activity of salivary amylase bound to the surface of several species of oral streptococci was determined by the production of acid from starch and by the...
The enzymatic activity of salivary amylase bound to the surface of several species of oral streptococci was determined by the production of acid from starch and by the degradation of maltotetraose to glucose in a coupled, spectrophotometric assay. Most strains able to bind amylase exhibited functional enzyme on their surface and produced acid from the products of amylolytic degradation. These strains were unable to utilise starch in the absence of salivary amylase. Two strains failed to produce acid from starch, despite the presence of functional salivary amylase, because they could not utilise maltose. Strains that could not bind salivary amylase failed to produce acid from starch. In no case was all the bound salivary amylase active, and two strains of Streptococcus mitis which bound amylase did not exhibit any enzyme activity on their cell surface. The ability to bind amylase may confer a survival advantage on oral bacteria which inhabit hosts that consume diets containing starch.
Topics: Acids; Adsorption; Amylases; Carbohydrate Metabolism; Humans; Saliva; Streptococcus
PubMed: 1376290
DOI: 10.1016/0378-1097(92)90511-l -
Applied Microbiology Apr 1970The effect of different media and pH on the formation of amylase by Aspergillus oryzae EI 212 is described. Depending upon the composition of the medium and growth...
The effect of different media and pH on the formation of amylase by Aspergillus oryzae EI 212 is described. Depending upon the composition of the medium and growth conditions, the fungus was found to secrete alpha- or beta-amylase, or both. Some of the properties of the partially purified alpha-amylase were found to be different from alpha-amylases from other sources.
Topics: Agar; Amylases; Asparagine; Aspergillus; Culture Media; Fermentation; Hydrogen-Ion Concentration; Molecular Weight; Starch; Temperature
PubMed: 5418942
DOI: 10.1128/am.19.4.598-603.1970 -
Postepy Higieny I Medycyny... 1979
Comparative Study Review
Topics: Amino Acids; Amylases; Animals; Carboxylic Acids; Catalysis; Chemical Phenomena; Chemistry; Chickens; Dogs; Guinea Pigs; Humans; Imidazoles; Isoenzymes; Mice; Pancreas; Polymorphism, Genetic; Rats; Swine
PubMed: 94945
DOI: No ID Found -
Journal of the American Pharmaceutical... May 1948
Topics: Amylases; alpha-Amylases
PubMed: 18865161
DOI: 10.1002/jps.3030370506