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Autres documents

T9378

Sigma-Aldrich

Trypsin inhibitor from Phaseolus limensis (lima bean)

Type II-L, crude powder

Synonyme(s) :

Trypsin Inhibitor from lima beans

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About This Item

Numéro CAS:
9035-81-8
Numéro CE :
232-906-9
Numéro MDL:
MFCD00082102
Code UNSPSC :
12352202
Nomenclature NACRES :
NA.77

Source biologique

Phaseolus limensis (lima bean)

Niveau de qualité

200

Type

Type II-L

Forme

crude powder

Poids mol.

9 kDa

Solubilité

0.067 M sodium phosphate buffer, pH 7.6: 1 mg/mL

Température de stockage

2-8°C

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Application

Trypsin inhibitor from Phaseolus limensis (lima bean) has been used:
  • in the inhibition of trypsin in human plasma
  • in the termination of proteolytic digestion in rabbit skeletal muscles
  • in the inhibition of salivary glands enzyme extract from Lygus lineolaris
  • in the inhibition of proteolytic activity in Agave tequilana enzyme extract

Trypsin inhibitor has been used as an affinity ligand for isolation of elastase-type enzymes.

Actions biochimiques/physiologiques

Trypsin inhibitor from lima beans belongs to Bowman-Birk family of protease inhibitors. It is 9 kDa in molecular weight and contains nine disulfide bridges and is highly thermostable. It has trypsin and chymotrypsin binding subdomains.

Propriétés physiques

Monomer has an apparent molecular weight of approx. 9,000 Da but undergoes a concentration and pH-dependent dimerization.

Définition de l'unité

One trypsin unit will produce a ΔA253 of 0.001 per min with BAEE as substrate at pH 7.6 at 25 °C; reaction volume 3.2 mL, 1 cm light path.

Notes préparatoires

Prepared by a modification of the method of Tauber, H., et al., J. Biol. Chem., 179, 1155 (1949) (modified).

Remarque sur l'analyse

One mg will inhibit ≥0.8 mg of trypsin with activity of approx. 10,000 BAEE units per mg protein.

Autres remarques

View more information on Trypsin Inhibitor.

Pictogrammes

Health hazard
GHS08

Mention d'avertissement

Danger

Mentions de danger

H317 - H334

Classification des risques

Resp. Sens. 1 - Skin Sens. 1

Code de la classe de stockage

11 - Combustible Solids

Classe de danger pour l'eau (WGK)

WGK 3

Point d'éclair (°F)

Not applicable

Point d'éclair (°C)

Not applicable

Équipement de protection individuelle

Eyeshields, Gloves, type N95 (US)

Certificats d'analyse (COA)

Recherchez un Certificats d'analyse (COA) en saisissant le numéro de lot du produit. Les numéros de lot figurent sur l'étiquette du produit après les mots "Lot" ou "Batch".

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Consulter la Bibliothèque de documents

G Bellon et al.
Artery, 7(4), 290-302 (1980-01-01)
A serine protease active on insoluble elastin at neutral pH has been isolated from human aortic media employing a Lima-bean trypsin inhibitor - Sepharose column. It is also hydrolyzed Suc (Ala)3 pna and casein but was found inactive against Benzoyl-Tyr-pna
In-house phase determination of the lima bean trypsin inhibitor: a low-resolution sulfur-SAD case
Debreczeni J, et al.
Acta crystallographica. Section D, Structural biology, 59(2), 393-395 (2003)
Are cardiovascular and sympathoadrenal effects of human ?new pressor protein? preparations attributable to human coagulation beta-FXIIa?
Papageorgiou PC, et al.
American Journal of Physiology. Heart and Circulatory Physiology, 286(3), H837-H846 (2004)
A Rapid and Reliable Method for Total Protein Extraction from Succulent Plants for Proteomic Analysis
Lledias F, et al.
The Protein Journal, 36(4), 308-321 (2017)
Shark skeletal muscle tropomyosin is a phosphoprotein
Hayley M, et al.
Journal of Muscle Research and Cell Motility, 29(2-5), 101-107 (2008)
Afficher tous les articles scientifiques apparentés

Articles

Chymotrypsin

Analytical Enzyme Chymotrypsin: Chymotrypsin is produced in the acinar cells of the pancreas as the inactive precursor, chymotrypsinogen.

Protocoles

Enzymatic Assay of Trypsin Inhibitor

This technical article described the Enzymatic Assay of Trypsin Inhibitor.

Contenu apparenté

Trypsin Serine Protease Enzyme

Trypsin is an enzyme in the serine protease class that consists of a polypeptide chain of 223 amino acid residues. Multiple sources, grades and formulations of trypsin specifically designed for research applications are available.

Chromatograms

application for HPLC

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