Purification and characterisation of collagenolytic cathepsins from rabbit liver

Mason, Robert W.; Taylor, Mark A.; Etherington, David J.

doi:10.1016/0014-5793(82)80699-6

Cited by 16 publications

(11 citation statements)

References 10 publications

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“…Similarly to cathepsin S, cathepsin N from beef spleen was also reported to have a lower activity towards Z-Phe-Arg-NMec than found for the rabbit liver isoenzymes of cathepsin L [15]. However, it has not been established whether cathepsin N from beef spleen degrades azocasein [ 161.…”

Section: Resultsmentioning

confidence: 99%

Species variations amongst lysosomal cysteine proteinases

1984

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Properties of cathepsin L from rat liver lysosomes were compared with those of a similar enzyme, cathepsin S from beef spleen. Major characteristics of cathepsin L are the high activity against Z-Phe-Arg-methylcoumarylamide and sensitivity to the fast reacting irreversible inhibitor Z-Phe-Phe-diazomethane.In contrast, cathepsin S hydrolyzes Z-Phe-Arg-methylcoumarylamide only slowly and Z-Phe-Phe-diazomethane cannot be regarded as a potent inhibitor of this enzyme. The differences in the substrate specificity of cathepsin L from rat liver and cathepsin S from beef spleen are discussed in comparison with the substrate specificity of cathepsin B from rat and human liver and beef spleen.

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Section: Resultsmentioning

confidence: 99%

Species variations amongst lysosomal cysteine proteinases

1984

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“…Cathepsin L (EC 3.4.22.15) was partially purified (to be free from cathepsin B activity) from rabbit liver, essentially using the method of Mason et al [12]. The purified material had an activity towards Bz-Pro-Phe-Arg-nan of 5 pmol/ min//zg protein.…”

Section: Methodsmentioning

confidence: 99%

Cystatin-like cysteine proteinase inhibitors of parasitic protozoa

Irvine

Coombs

North

1992

FEMS Microbiology Letters

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A new method has been developed for detecting cystatins and other cysteine proteinase inhibitors. The method, which involves protein separation by SDS‐PAGE followed by a cysteine proteinase overlay step, is more sensitive than previously reported techniques: as little as 1 ng of recombinant human cystatin C can be detected and cysteine proteinase inhibitors could also be detected in complex protein mixtures such as bovine foetal serum. The method has been used to show, for the first time, cysteine proteinase inhibitors in lysates of a range of parasitic protozoa (Trypanosoma brucei, Leishmania mexicana mexicana, Toxoplasma gondii and Tritrichomonas foetus) and to confirm that one occurs in the free‐living ciliate Tetrahymena pyriformis. Cystatin‐like inhibitory activity was also demonstrated in boiled lysates of L. mexicana mexicana using conventional assays methods.

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“…One reason for this may be that the values are dependent on incubation conditions and determination methods (e.g. concentration of trichloroacetic acid, incubation time in assays containing azo-casein and urea, concentrations of enzyme and substrate in the assay, source of proteins), as discussed by Mason et al (1982) and .…”

Section: Iu-mentioning

confidence: 99%

Cathepsin S from bovine spleen. Purification, distribution, intracellular localization and action on proteins

Kirschke

Wiederanders

Brὂmme

et al. 1989

Biochemical Journal

189

115

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Cathepsin S was detected in bovine kidney, spleen, lymph nodes and lung by immunochemical methods. The immunostaining of cathepsin S in kidney was concentrated to the cells of the proximal tubule, where the enzyme was present in cytoplasmic granules. The purification method for cathepsin S from bovine spleen involved (NH4)2SO4 fractionation, chromatography on CM-Sephadex C-50, gel filtration on Sephacryl S-200 and chromatofocusing (pH 8.0-6.0). The enzyme was partially destroyed by autolysis of the homogenate at pH 4.2. The isoelectric point of cathepsin S was 7.0. Cathepsin S was found to hydrolyse proteins at a similar rate to cathepsin L below pH 7.0. At pH values of 7.0-7.5 cathepsin S retained most of its activity, whereas cathepsin L was completely inactive.

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Purification and characterisation of collagenolytic cathepsins from rabbit liver

Cited by 16 publications

References 10 publications

Species variations amongst lysosomal cysteine proteinases

Species variations amongst lysosomal cysteine proteinases

Cystatin-like cysteine proteinase inhibitors of parasitic protozoa

Cathepsin S from bovine spleen. Purification, distribution, intracellular localization and action on proteins

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