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By EriC.D. Wills (Auth.)

Publication by means of Wills, Eric D

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It must be appreciated that not all these enzymes have been detected in mammalian peroxisomes, some having, so far, been detected only in plants or protozoa. The system proposed assumes that coupling takes place between a group of oxidases producing H 2 0 2 (A) and a group of reactions (B) catalysed by catalase acting, in the presence of H 2 0 2 , as a peroxidase. This system is believed to occur in most peroxisomes including mammalian peroxisomes. The oxidation of ethanol and formate are likely to be of the greatest metabolic importance in mammals.

Within the lysosome, however, the pH may be much more acid. The reason for the acid pH optima of lysosomal enzymes is not at all clear; it may serve as a protective mechanism, rendering an enzyme relatively inactive should it leak out into a normally functioning cell. d. Sulphydry 1 enzymes Some of the lysosomal enzymes, especially the cathepsins, must have at least one, and sometimes several, free —SH groups of cysteine residues for full activity. Such enzymes are termed 'sulphydryF or —SH enzymes.

4, where slices of spleen and thymus tissue have been specifically stained to localize ROLE OFSUBCELLULAR ORGANELLES: LYSOSOMES 39 Fig. 4. Histochemical staining of lysosomes in (a) spleen and (b) thymus. Sections of tissue (8-μ,πι thick) are incubated in glycerol 3-phosphate medium as a substrate for acid phosphatase. Enzyme activity is shown by intense dark stain. Note the relatively small numbers of cells (macrophages) that stain intensely. The other cells in the tissues have very small numbers of weakly active lysosomes.

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