1159-15-5Relevant articles and documents
USE OF OPEN-CHAIN CARBOXYLIC ACIDS, CARBONIC ESTERS, CARBOXAMIDES AND CARBONITRILES OF ARYL, HETEROARYL AND BENZYLSULFONAMIDE OR THE SALTS THEREOF FOR IMPROVING THE STRESS TOLERANCE IN PLANTS
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Paragraph 0169-0170; 0173; 0343, (2014/02/15)
The invention relates to the use of open-chain aryl-, heteroaryl- and benzylsulfonamidocarboxylic acids, -carboxylic esters, -carboxamides and -carbonitriles or salts thereof of the formula (I) in which the respective substituents have the meanings given
Purification and characterization of trypsin from the spleen of tongol tuna (Thunnus tonggol)
Klomklao, Sappasith,Benjakul, Soottawat,Visessanguan, Wonnop,Kishimura, Hideki,Simpson, Benjamin K.
, p. 5617 - 5622 (2007/10/03)
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°C. It was stable in a wide pH range of 6-11 but unstable at the temperatures greater than 50°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 N α-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.