Detail of > 9000-90-2
- MSDS Download

- CAS Number:
- 9000-90-2
- Name:
Amylase, α-
- Superlist Name:
- alpha-Amylase
- Formula:
- Unspecified
- Synonyms:
- Amylase, alpha-;Fortizyme;Pancreatic amylase;UNII-I909J9CFAT;alpha-Amylase (swine pancreas);alpha Amylase [USAN];
- EINECS:
- 232-565-6
- Melting Point:
- 66-73 °C
- Appearance:
- yellow-brown lyophilized powder
- Hazard Symbols:
Xn,
B- Risk Codes:
- 42
- Safety:
- 36-36/37-24-22-45-2-23Details
- Deleted CAS:
- 9001-95-0|9036-05-9|9077-78-5|70356-39-7|106009-10-3|135319-50-5|144133-13-1
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Reference
- Comparative characteristics of membrane digestion in cestodes and in their hosts, fishes
- Comparative characteristics of membrane digestion in cestodes and in their hosts, fishes. Kuz'mina, V. V.; Kuperman, B. I. (Inst. Biol. Vnutr. Vod, Borok, USSR). Parazitologiya, 17(6), 436-42 (Russian) 1983. CODEN: PAZGA4. ISSN: 0031-1847. DOCUMENT TYPE: Journal CA Section: 12 (Nonmammalian Biochemistry) The invertase, a-amylase, and alk. phosphatase activities of the tegument membranes of Eubothrium rugosum in several host fish (Lota lota, Triaenophorus nodulosus, and Esox lucius) were detd. The level of carbohydrase activity was lower and that of alk. phosphatase was higher in the cestode than in the intestinal mucosa of the host fish. 9000-90-2 and 9001-78-9 are also in the experiment. There was also a difference in the levels of enzyme activity in the cestode dependent on the enzyme activity levels in the host intestinal mucosa. The desorption dynamics of the enzymes participating in the membrane digestion from the surface of the helminths were similar to those of the host fish, suggesting a similarity in the structural-functional organization of their digestive-transport surface. Differences were found in the activity rates of the carbohydrases in various parts of the cestodes strobilia. Carbohydrase levels were highest in the middle regions, whereas alk. phosphatase levels were highest in the posterior regions. Apparently, the enzymic app. of cestodes adapts to the food content of the host fish. .
- High a-amylase activity in the syncytiotrophoblastic cells of first-trimester human placentas
- High a-amylase activity in the syncytiotrophoblastic cells of first-trimester human placentas. Fisher, Susan J.; Laine, Roger A. (Coll. Med., Univ. Kentucky, Lexington, KY 40536, USA). J. Cell. Biochem., 22(1), 47-54 (English) 1983. CODEN: JCEBD5. ISSN: 0730-2312. DOCUMENT TYPE: Journal CA Section: 13 (Mammalian Biochemistry) The syncytiotrophoblastic brush border of the human placenta forms the maternal-fetal interface and is an important determinant of placental function. Electron micrographs of fresh brush border prepns. isolated from 1st-trimester human placenta showed membrane vesicles, open-ended microvilli, and numerous glycogen particles. Anal. of the microvillar membranes for several plasma and intracellular membrane markers showed a high degree of purifn., comparable to the results reported for the isolation of microvilli from full-term human placentas. The microvillar prepns. from 1st-trimester placentas, however, also contained the enzymes necessary to synthesize and degrade glycogen. The degrdn. resulted in the accumulation of maltotriose and maltotetraose, apparently due to the action of a liver-type a-amylase. The occurrence of this enzyme and the enzymes for synthesizing glycogen in this brush border fraction is probably assocd. with the necessity for an extremely active glucose transport and liver-like storage system within the fetal tissue at this fetal-maternal membrane interface.Except for chemicals metioned above, 34612-38-9 and 9000-90-2 are also used. .
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