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Trypsin Inhibitor Soybean (C007B-279330)

Catalog No.
C007B-279330
Manufacturer No.
T113170-500mg
Manufacturer Name
Aladdin Scientific
Quantity
1
Unit of Measure
EA

Molecular weight: 21,500 ± 800 (Wu and Scheraga 1972a).Optimum pH: 7.0.Composition: The Kunitz soybean inhibitor consists of a single polypeptide chain crosslinked by two disulfide bridges (Steiner 1965). Structural studies of the inhibitor and

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Molecular weight: 21,500 ± 800 (Wu and Scheraga 1972a).Optimum pH: 7.0.Composition: The Kunitz soybean inhibitor consists of a single polypeptide chain crosslinked by two disulfide bridges (Steiner 1965). Structural studies of the inhibitor and active site have been reported, Ellis et al. (1975), Woodward and Ellis (1975), Koide et al. (1974), Koide and Ikenaka (1973), Bidlingmeyer et al. (1972), Ikenaka et al. (1971), Papaioannou and Liener (1970), Hixson and Laskowski (1970), Kato and Tominager (1970), and Wu and Scherage (1962). Donovan and Beardslee (1975) have reported on the thermal denaturation of inhibitor complexes.Isoelectric point: 4.5 (Kunitz 1947).Specificity: Soybean inhibitor inhibits trypsin mole-for-mole and to a lesser extent chymotrypsin. (Bidlingmeyer et al. 1972). Lanchantin et al. (1969) report soybean inhibitor to form a one-to-one complex with beef or human thrombin thus blocking its specific proteolytic capacity to activate prothrombin. Nanninga and Guest (1964) report plasmin to be inhibited. STI has been reported to inhibit leukocytic proteases. (Lieberman and Gawad 1971), but not the esterolytic, proteolytic or elastolytic activities of porcine elastase (Gertler and Feinstein 1971).Soybean Trypsin Inhibitor (Kunitz):Soybean trypsin inhibitor (SBTI) first crystallized by Kunitz (1945) is one of several such inhibitors found in soybeans. (Fratalli 1969; Millar et al. 1969; Fratalli and Steiner 1968; Birk et al. 1967). The best known preparation is that of Kunitz. Steiner and Fratalli (1969) have reviewed the Kunitz and Bowman-Birk inhibitors. A protein (or polypeptide) proteinase inhibitor probably has peptide bonds compatible with the protease reactive site. Finkenstadt and Laskowski (1965 and 1967) and Ozawa and Laskowski (1966) indicate that a single Arg-Ile bond is cleaved by trypsin; a covalent bimolecular complex of inhibitor and trypsin results. On dissociation either virginal or modified inhibitor appears; see Hixson and Laskowski (1970a), Isheda et al. (1970) and Niekamp et al. (1969).Enzyme activity definition:The activity of the inhibitors is expressed as the amount of twice crystallized trypsin (Aladdin Item: T128774) inhibited per milligram of inhibitor. 1mg trypsin ≥180 TAME units, 10,350 BAEE units, 3,450 USP/NF units.

Specifications and Purity: Animal Free, From Soybean

MDL Number: MFCD00082102

EC Number: 232-906-9

Related Documents: https://aladdin-for-icloud-store.oss-cn-hangzhou.aliyuncs.com/aladdinsci/pdp/sds/1/T113170-SCI_20770c43941880179736b27dad435adc.pdf

UPC:
51181906
Condition:
New
HazmatClass:
No
WeightUOM:
LB
MPN:
T113170-500mg
CAS:
9035-81-8
Product Size:
500mg
Hazard Statement Codes:
H334:H317
Precautionary Statement Codes:
P342+P311:P280:P261

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