Abstract
THE histochemical visualization of a calcium activated N(α-L-glutamyl)β-naphthylamide-cleaving activity has been described in an earlier publication1. Hydrolysis of N(α-L-aspartyl)β-naphthylamide has now been observed histochemically in sites identical to those described for N(α-L-glutamyl)β-naphthyl-amide (for example, guinea pig pancreatic duct epithelium and islets of Langerhans and human and rat glomeruli) in the presence of the optimal concentration of the activating ion, calcium. The above tissue section localizations of the enzymatically catalysed hydrolysis of the α-L-glutamyl and α-L-aspartyl substrates are distinct from those seen with other β-naphthylamide substrates in the presence of calcium ions.
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References
Glenner, G. G., and Folk, J. E., Nature, 192, 338 (1961).
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Glenner, G. G., Folk, J. E., and McMillan, P. J., J. Histochem. Cytochem. (in the press).
Folk, J. E., and Burstone, M. S., Proc. Soc. Exp. Biol. Med., 89, 473 (1955).
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GLENNER, G., McMILLAN, P. & FOLK, J. A Mammalian Peptidase specific for the Hydrolysis of N-Terminal α-L-Glutamyl and Aspartyl Residues. Nature 194, 867 (1962). https://doi.org/10.1038/194867a0
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DOI: https://doi.org/10.1038/194867a0
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