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Detail of "9078-38-0"

  • CAS Number:
  • 9078-38-0
  • Name:
  • Trypsin inhibitor,soybean

  • Molecular Weight:
  • 6511.83
  • Synonyms:
  • SBTI; STI;Soybean trypsin inhibitor; Trypsin inhibitor SBTI
  • EINECS:
  • 232-987-0
  • Solubility:
  • >10 mg/mL

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CAS No.9078-38-0 TRYPSIN INHIBITOR

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Supplier:Worthington Biochemical Corporation [ United States]

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Reference

The effect of feeding soybean trypsin inhibitor and repeated injections of cholecystokinin on rat pancreas
The effect of feeding soybean trypsin inhibitor and repeated injections of cholecystokinin on rat pancreas. Temler, Roman S.; Dormond, Charles A.; Simon, Eliane; Morel, Brigitte (Nestle Res. Dep., La Tour-de-Peilz CH-1814, Switz.). J. Nutr., 114(6), 1083-91 (English) 1984. CODEN: JONUAI. ISSN: 0022-3166. DOCUMENT TYPE: Journal CA Section: 2 (Mammalian Hormones) The effects of dietary soybean trypsin inhibitor (SBTI, Kunitz type) [9078-38-0] or repeated i.p. injections of 95% pure cholecystokinin-39 (CCK-39) [79955-77-4] on rat pancreas were investigated in a 10-day expt. SBTI and CCK-39 induced similar increases in pancreatic wt., which led to both cellular hypertrophy and hyperplasia. Trypsin [9002-07-7] and chymotrypsin [9004-07-3] activity increased with an increase in pancreatic wt. Amylase [9000-92-4] activity increased only after CCK-39 injection, whereas lipase activity was not affected by either SBTI or CCK-39 treatment. After both treatments, insulin [9004-10-8] content showed only a slight tendency to increase, whereas glucagon [9007-92-5] content was not different from controls. SBTI and CCK-39 mainly exert their effects on the exocrine pancreas in a similar, but not identical, manner. Thus, SBTI is not only a potent stimulator of the secretion of cholecystokinin activity but also of other unidentified gastrointestinal factor(s).
Effects of protease inhibitors on the autolysis and protease activities of Antarctic krill
Effects of protease inhibitors on the autolysis and protease activities of Antarctic krill. Kawamura, Yukio; Nishimura, Kimio; Matoba, Teruyoshi; Yonezawa, Daizo (Res. Inst. Food Sci., Kyoto Univ., Uji 611, Japan). Agric. Biol. Chem., 48(4), 923-30 (English) 1984. CODEN: ABCHA6. ISSN: 0002-1369. DOCUMENT TYPE: Journal CA Section: 17 (Food and Feed Chemistry) To det. which protease [9001-92-7] are responsible for the autolysis of krill, the effects of several protease inhibitors on the autolysis and protease activities of krill were investigated. Homogenates of whole bodies, and the cephalothorax and abdomen parts of frozen krill were equilibrated at 37° at different pHs between 2 to 10 and allowed to stand for 16 h, following which the increase in the TCA sol. fraction was monitored. 14C-Hb hydrolyzing activity was also measured using each homogenate as a crude enzyme prepn. The degree of autolysis and the 14C-Hb hydrolyzing activity were max. at pH 5-8 for the parts studied. The hydrolytic activity was highest in the cephalothorax, followed by that in the whole body and then the abdomen. The effects of inhibitors on the 14C-Hb hydrolyzing activity were examd. Soybean trypsin inhibitor (STI) [9078-38-0], diisopropyl fluorophosphate [55-91-4], and leupeptin inhibited the activity at neutral pH, and pepstatin [26305-03-3], monoiodoacetic acid [64-69-7], and leupeptin were effective at acidic pH for all the parts. Investigation of the effects of inhibitors on the autolysis at 20° at pH 4 and 7 by SDS-polyacrylamide gel electrophoresis indicated that the autolysis of the cephalothorax and whole body at pH 7 was suppressed a little by STI and the autolysis of the abdomen and whole body at pH 4 was significantly inhibited by iodoacetamide and leupeptin. Apparently, the main proteases responsible for the autolysis of krill are trypsin [9002-07-7] like-proteases at neutral pH and cathepsins (B [9047-22-7], H [60748-73-4], and L [60616-82-2] types) at acidic pH.
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