Summary
Cathepsin B has been purified by gel filtration. A complete separation from cathepsin C and D was achieved. This particular proteinase hydrolysed the chromogenic substrates BANA and LNA. Cathepsin B must thus be included among the potential initiators of a positive histochemical LNase reaction.
Similar content being viewed by others
References
Haba, G. de la, P. S. Cammarata, and S. N. Timasheff: The partial purification and some physical properties of cathepsin C from beef spleen. J. biol. Chem. 234, 316–319 (1959).
Smith, E. L., and D. H. Spackman: Leucine aminopeptidase. V. Activation, specificity, and mechanism of action. J. biol. Chem. 212, 271–299 (1955).
Snellman, O., and B. Sylvén: Haptoglobin acting as a natural inhibitor of cathepsin B activity. Nature (Lond.) 216, 1033 (1967).
Sylvén, B., and I. Bois: Studies on the histochemical “leucine aminopeptidase” reaction. I. Identity of the enzymes possibly involved. Histochemie 3, 65–78 (1962).
, and I. Bois-Svensson: Studies on the histochemical “leucine aminopeptidase” reaction. IV. Chemical and histochemical characterization of the intracellular and stromal LNA reactions in solid tumor transplants. Histochemie 4, 135–149 (1964).
and O. Snellman: A new metal-dependent enzyme present in cathepsin C preparations. Biochim. biophys. Acta (Amst.) 65, 350–353 (1962).
: Studies on the histochemical “leucine aminopeptidase” reaction. III. On the different LNA-splitting enzymes from spleen. Histochemie 3, 484–486 (1964).
Vanha-Perttula, T. P. J., and V. K. Hopsu: The ovarial enzymes hydrolysing L-leucyl and DL-alanyl-β-naphthylamide. Histochemie 6, 34–45 (1966).
Author information
Authors and Affiliations
Additional information
Supported by grants from the Jubilee Fund, Cancer Society of Stockholm and the Swedish Natural Research Council.
Rights and permissions
About this article
Cite this article
Sylvén, B., Snellman, O. Studies on the histochemical “leucine aminopeptidase” reaction. Histochemie 12, 240–243 (1968). https://doi.org/10.1007/BF00306001
Received:
Issue Date:
DOI: https://doi.org/10.1007/BF00306001