Home
Resources
Publications
Purification and Characterization of Trypsin From the Spleen of Tongol Tuna (Thunnus Tonggol)

Purification and Characterization of Trypsin From the Spleen of Tongol Tuna (Thunnus Tonggol)

Sappasith Klomklao, Soottawat Benjakul, Wonnop Visessanguan, Hideki Kishimura, Benjamin K Simpson

J Agric Food Chem. 2006 Jul 26;54(15):5617-22.

PMID: 16848554

Abstract:

Trypsin from tongol tuna (Thunnus tonggol) spleen was purified to 402-fold by ammonium sulfate precipitation, followed by a series of chromatographic separations. The molecular mass of trypsin was estimated to be 24 kDa by size-exclusion chromatography and sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE). Trypsin appearing as a single band on native PAGE showed the maximal activity at pH 8.5 and 65 degrees C. It was stable in a wide pH range of 6-11 but unstable at the temperatures greater than 50 degrees C. The enzyme required calcium ion for thermal stability. The activity was strongly inhibited by 1.0 g/L soybean trypsin inhibitor and 5 mM TLCK and partially inhibited by 2 mM ethylenediaminetetraacetic acid. Activity was lowered with an increasing NaCl concentration (0-30%). The enzyme had a Km for Nalpha-p-tosyl-L-arginine methyl ester hydrochloride of 0.25 mM and a Kcat of 200 s-1. The N-terminal amino acid sequence of trypsin was determined as IVGGYECQAHSQPHQVSLNA and was very homologous to other trypsins.

Chemicals Related in the Paper:

Catalog Number	Product Name	Structure	CAS Number	Price
AP1784038	Nα-p-Tosyl-L-arginine methyl ester hydrochloride		1784-03-8	Price

As a specialist in analytical chemical Products, Alfa Chemistry offers consumers a wealth of raw materials and a full range of technologies and services.

QUICK LINKS

HEADQUARTERS

Tel:

Fax:

Email: