. The Biological bulletin. Biology; Zoology; Biology; Marine Biology. 606 PETER W. PAPPAS AND CLARK P. READ Hammersten casein (Sigma and Mann Research Chemicals, respectively) as sub- strates using the methods of Bergmeyer (1903). Assays, using azoalbumin as a substrate, were also conducted in which worms were pre-incubated in the KRT-enzyme solution for 15 min, and not removed before the addition of substrate (, worms were in the assay medium for the 15 min pre-incubation and 30 min assay periods). Previous control experiments (Pappas and Read, 1972) have demonstrated that H. diiniintta d


. The Biological bulletin. Biology; Zoology; Biology; Marine Biology. 606 PETER W. PAPPAS AND CLARK P. READ Hammersten casein (Sigma and Mann Research Chemicals, respectively) as sub- strates using the methods of Bergmeyer (1903). Assays, using azoalbumin as a substrate, were also conducted in which worms were pre-incubated in the KRT-enzyme solution for 15 min, and not removed before the addition of substrate (, worms were in the assay medium for the 15 min pre-incubation and 30 min assay periods). Previous control experiments (Pappas and Read, 1972) have demonstrated that H. diiniintta does not absorb or adsorb measurable amounts of the TCA-solution products of azoalbumin digestion. 140 r. .2 .3 .4 FIGURE 1. A plot of velocity (V, color change/30 min assay) of azoalbumin hydrolysis versus substrate concentration ([S], % azoalbumin) by a-chymotrypsin with (open circles) and without (solid circles) a 15 min pre-incubation with Hymenolepis dhninuta and /3-chymo- trypsin with (open squares) and without (solid squares) a 15 min pre-incubation with Hy- menolepis dhninnta. Lines were fitted by inspection. Experiments were conducted in which worms were incubated in KRT for 15 min, and removed, followed by the addition of either a- or /?-chymotrypsin and substrate to this same KRT. These assays demonstrated that neither enzyme was affected by excretory/secretory products of the worms. Worms have also been shown previously to lack intrinsic proteolytic activity (Pappas and Read, 1972). Experiments were performed to determine whether H. dhninuta inactivates a-chymotrypsinogen A (Sigma Type II, from bovine pancreas; BTEE units/ nig prior to activation, 56 BTEE units/nig following activation with trypsin). Preliminary experiments were run to insure that the a-chymotrypsinogen A was. Please note that these images are extracted from scanned page images that may have been digitally enhanced for readability - coloration and appearance of these illustrations may not perfec


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Keywords: ., bookauthorlilliefrankrat, booksubjectbiology, booksubjectzoology