Product Name
Trypsin inhibitor from Phaseolus limensis (lima bean), Type II-L, crude powder
biological source
Phaseolus limensis (lima bean)
type
Type II-L
form
crude powder
mol wt
9 kDa
solubility
0.067 M sodium phosphate buffer, pH 7.6: 1 mg/mL
storage temp.
2-8°C
Quality Level
Looking for similar products? Visit Product Comparison Guide
Analysis Note
One mg will inhibit ≥0.8 mg of trypsin with activity of approx. 10,000 BAEE units per mg protein.
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.
Biochem/physiol Actions
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.
General description
Monomer has an apparent molecular weight of approx. 9,000 Da but undergoes a concentration and pH-dependent dimerization.
Other Notes
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.
View more information on Trypsin Inhibitor.
Preparation Note
Prepared by a modification of the method of Tauber, H., et al., J. Biol. Chem., 179, 1155 (1949) (modified).
signalword
Danger
hcodes
Hazard Classifications
Resp. Sens. 1 - Skin Sens. 1
Storage Class
11 - Combustible Solids
wgk
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, type N95 (US)
Choose from one of the most recent versions:
Already Own This Product?
Find documentation for the products that you have recently purchased in the Document Library.
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)
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)
Shark skeletal muscle tropomyosin is a phosphoprotein
Hayley M, et al.
Journal of Muscle Research and Cell Motility, 29(2-5), 101-107 (2008)
Malik Shoaib Ahmad et al.
Proteins, 91(1), 22-31 (2022-08-05)
Bovine pancreatic trypsin was crystallized, in-complex with Lima bean trypsin inhibitor (LBTI) (Phaseolus lunatus L.), in the form of a ternary complex. LBTI is a Bowman-Birk-type bifunctional serine protease inhibitor, which has two independent inhibitory loops. Both of the loops
Partial characterization of trypsin-like protease and molecular cloning of a trypsin-like precursor cDNA in salivary glands of Lygus lineolaris
Zeng F, et al.
Comparative Biochemistry and Physiology. Part B, Biochemistry & Molecular Biology, 131(3), 453-463 (2002)
Related Content
Product Information Sheet
QC Methods
Our team of scientists has experience in all areas of research including Life Science, Material Science, Chemical Synthesis, Chromatography, Analytical and many others.
Contact Technical Service