Reference

Cell walls of Phaseolus vulgaris leaves contain the Azocoll-digesting proteinase

Cell walls of Phaseolus vulgaris leaves contain the Azocoll-digesting proteinase. Van der Wilden, Willem; Segers, Johannus H. L.; Chrispeels, Maarten J. 53092-90-3 and 9001-92-7 are also occured in this study. (Dep. Biol., Univ. California, San Diego, La Jolla, CA 92093, USA). Plant Physiol., 73(3), 576-8 (English) 1983. CODEN: PLPHAY. ISSN: 0032-0889. DOCUMENT TYPE: Journal CA Section: 11 (Plant Biochemistry) Section cross-reference(s): 7 The leaves of P. vulgaris contain an endopeptidase with a pH optimum of 9.0 and an isoelec. point between 10.0 and 10.5. This endopeptidase is the only abundant Azocoll-digesting proteinase in the leaves. The activity of this enzyme is highest in immature leaves and declines as the leaf matures and senesces. Enzymically isolated protoplasts contain very little of this proteinase. The proteinase can be recovered readily from the extracellular fluid obtained by gentle centrifugation of leaf strips vacuum-infiltrated with a buffered soln. The Azocoll-digesting proteinase is located in the periplasmic space and (or) the cell wall. .

Evaluation of chromogenic substrates for measurement of protease production by biocontrol strains of Trichoderma

Evaluation of chromogenic substrates for measurement of protease production by biocontrol strains of Trichoderma. Mischke, Sue (Systematic Botany Mycol. Lab., Agric. Research Service, U.S. Department of Agriculture, Beltsville, MD 20705-2350, USA). Microbios, 87(352), 175-183 (English) 1996 Faculty Press. CODEN: MCBIA7. ISSN: 0026-2633. DOCUMENT TYPE: Journal CA Section: 7 (Enzymes) Section cross-reference(s): 10 Four chromogenic substrates were compared, and methods were developed for measuring protease activity from fungi. Digestion of azoalbumin, a water-sol. substrate, resulted in dye release most closely proportional to enzyme activity. Substrates insol. in water were advantageous for time-course studies, and azocoll was more sensitive to digestion and easier to handle than hide powder azure. The optimal pH was 7 for measurement of extracellular protease activity from the Trichoderma strains. 12679-76-4 and 53092-90-3 which are cas registry numbers of substances are two of reagents here. Addn. of calcium or serine protease inhibitors did not affect crude protease activity. The optimized protocol was used to demonstrate that specific activity of proteases produced by the strains of Trichoderma tested did not correlate with their known biocontrol ability. .