Trypsin, Bovine Pancreas, TPCK Treated

Trypsin is a pancreatic serine protease with substrate specificity based upon positively charged lysine and arginine side chains (Brown and Wold, 1973a). It has been isolated from a number of sources including dogfish (Titani, et al., 1975), moose (Stevenson and Voordouw, 1975), whale (Bricteux-Gregoire, et al., 1975), elephant seal (Bricteux-Gegoire, et al., 1974), Streptomyces griseus (Jurasek and Smillie, 1974; Olafson and Smillie, 1975), canine (Ohlsson and Tegner, 1973), African lungfish (Reeck and Neurath, 1972), swine (Hermodson, et al., 1973; Walker and Keil, 1973), rat (Vandermeers, et al., 1973), human ( Mallory and Travis, 1973; Figarell, et al., 1975). Trypsinogen and trypsin have been reviewed by Walsh (1970). The enzyme exhibits esterase and amidase activities.\n\nActivity (Dry Weight): \n(same/more than)180 units per mg Dry Weight\n\nActivity (Protein): \n(same/more than)180 units per mg protein\n\nUnit Definition:\n1 unit hydrolyzes 1 umole of p-toluene-sulfonyl-L-arginine methyl ester (TAME) per minute at 25C, pH 8.2, in the presence of 0.01M calcium ion. (1 TAME unit = 19.2 USP/NF units = 57.5 BAEE units).\n\nChymotrypsin: (same/less than) 0.02%\n\nProtein: (same/more than) 80%\n\nQuality Control: SDS-PAGE\n\nCharacteristics of Trypsin from Bovine Pancreas:\nMW:\nTrypsinogen: 24,000D (Walsh and Neurath, 1964).\nTrypsin: 23,800D (Cunningham, 1954).\n\nOptimum pH: ~8.0.\n\nExtinction coefficient: = 14.3.\n\nIsoelectric point:\nTrypsinogen: pH 9.3 (Walsh and Neurath, 1964).\nTrypsin: pH 10.5 (Cunningham, 1954).\n\nComposition: Trypsinogen has been shown to have certain intrinsic activity. See Knights and Light (1974) for further references. It is usually considered as the inactive precursor of trypsin which may be activated by removal of a terminal hexapeptide to yield single-chain [[beta]]-trypsin. Subsequent limited autolysis produces other active forms having two or more peptide chains bound by disulfide bonds. The predominant forms are [[alpha]]-trypsin, having two peptide chains and [[beta]]-, a single chain. Different activity and thermal stability are shown by [[alpha]]-and [[beta]]-trypsin.\n\nBenzamidine prevents conversion of [[beta]] to [[alpha]] (Beardslee and Zahnley, 1973; Schroeder and Shaw, 1968). Trypsin can, by chromatography, be separated into the [[alpha]] and [[beta]] forms. (Jameson and Elmore, 1974). See also Keil-Dlouh

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SPECIFICATIONS

Catalog Number

T8674

Size

100mg

Form

Supplied as a lyophilized powder that has been treated with L-(tosylamido-2-phenyl) ethyl chloromethyl ketone (TPCK) to inhibit contaminating chymotryptic activity.

Purity

Chromatographically purified

References

US Biological application reference: Gainey, M.R. et al., (2009) Health 2:32-37. 1. Abita, J., and Lazdunski, M.: On the Structural and Functional Role of Carboxylates in Chymotrypsinogen A: A Comparison with Chymotrypsin, Trypsinogen and Trypsin, Biochem. Biophys. Res. Comm., 35, 707 (1969). 2. Abuchowski, A., and Davis, F.: Preparation and Properties of Polyethylene Glycol-Trypsin Adducts, Biochim. Biophys. Acta, 578, 41 (1979). 3. Anson, M.: The Estimation of Pepsin, Trypsin, Papain and Cathepsin with Hemoglobin, J. Gen. Physiol., 22, 79 (1938). 4. Antonini, E., and Ascenzi, P.: The Mechanism of Trypsin Catalysis at Low pH. Proposal for a Structural Model, J. Biol. Chem., 256, 12449 (1981). 5. Arakawa, T., Hung, L., Mcginley, M., Rohde, M., and Narhi, L.: Induced Resistance of Trypsin to Sodium Dodecylsulfate upon Complex Formation with Trypsin Inhibitor, J. Protein Chem., 11, 171 (1992). 6. Arnon, R., and Neurath, H.: An Immunological Approach to the Study of Evolution of Trypsins, Proc. Natl. Acad. Sci., 64, 1323 (1969). 7. Ascenzi, P., Amiconi, G., Bolognesi, M., Menegatti, E., and Guarneri, M.: Trypsin Activation. Effect of the Ile-Val Dipeptide Concentration on Kazal Inhibitor Binding to Bovine Trypsinogen, Biochim. Biophys. Acta, 832, 1985 (1985).\n\nAscenzi, P., Bolognesi, M., Guarneri, M., Menegatti, E., and Amiconi, G.: Benzamidine as a Spectroscopic Probe for the Primary Specificity Subsite of Trypsin-like Proteinases, Mol. Cell.\nBiochem., 64, 139 (1984).\n\nAscenzi, P., Menegatti, E., Bortolotti, F., Guarneri, M., and Antonini, E.: Steady-state and Pre-steady-state Kinetics of the Trypsin-catalyzed Hydrolysis of a-CBZ-L-Lysine-p-nitrophenyl Ester,\nBiochim. Biophys. Acta, 658, 158 (1981).\n\nAsgeirsson, B., Fox, J., and Bjarnason, J.: Purification and Characterization of Trypsin from the Poikilotherm Gladus morhua, Eur. J. Biochem., 180, 85 (1989).\n\nAtassi, P.: Surface-simulation Synthesis of the Substrate-binding Site of an Enzyme. Demonstration with Trypsin, Biochem. J., 226, 477 (1985).\n\nBaines, N., Baird, J., and Elmore, D.: The Kinetics of Hydrolysis of Derivatives of Arginine, Homoarginine and Ornithine by Trypsin, Biochem. J., 90, 470 (1964).\n\nBalls, A.: Concerning Trypsinogen, Proc. Natl. Acad. Sci., 53, 392 (1965).\n\nBar-Eli, A., and Katchalski, E.: Water-Insoluble Trypsin Derivative and its Use as a Trypsin Column, Nature, 188, 856 (1960).\n\nBartholomew, J., Handley, C., and Lowther, D.: The Effects of Trypsin Treatment on Proteoglycan Biosynthesis of Bovine Articular Cartilage, Biochem. J., 227, 429 (1985).\n\nBeardslee, R., and Zahnley, J.: A Simple Preparation of [[beta]]-Trypsin Based on a Colorimetric Study of the Thermal Stabilities of [[alpha]] and [[beta]] Trypsin, Arch. Biochem. Biophys., 158,\n806 (1973).\n\nBerezin, I., Kazanskaya, N., Klyosov, A., and Svedas, V.: The Mechanism of the [[alpha]]-Chymotrypsin and Trypsin-Catalyzed Hydrolysis of Amides. Evidence for the Participation of the Active\nSerine in the Amidase Activity of Trypsin, Eur. J. Biochem., 38, 529 (1973).\n\nBergmann, M., and Fruton, J.: in Advances in Enzymology, 63 (1941).\n\nBerlin, I., and Neujahr, H.: Studies of Controlled Lysis of Washed Cell Suspensions of Lactobacillus fermenti and Preparation of Membrane-like Fragments by a Combined Trypsin-Lysozyme\nTreatment, Acta Chem. Scand., 22, 2972 (1969).\n\nBerliner, L., and Wong, S.: Evidence Against Two \"pH-locked\" Conformations of Phosphorylated Trypsin, J. Biol. Chem., 248, 1118 (1973).\n\nBerliner, L., and Wong, S.: Spin-Labeled Sulfonyl Fluorides as Active Site Probes of Protease Structure. I. Comparison of the Active Site Environments in [[alpha]]-Chymotrypsin and Trypsin, J.\nBiol. Chem., 249, 1668 (1974).\n\nBier, M., and Nord, F.: Arch. Biochem. Biophys., 33, 320 (1951).\n\nBorovsky, D., and Schlein, Y.: Quantitative Determination of Trypsin-like and Chymotrypsin-like Enzymes in Insects, Arch. Insect Biochem. Physiol., 8, 249 (1988).\n\nBricteux -Gr

Alternative Names

EC=3.4.21.4