Abstract
IT has been found that a Carboxypeptidase (or a mixture of various carboxypeptidases) occurs in the peel of citrus fruit, for example, of the orange (Citrus sinensis), lemon (Citrus medica), and grapefruit (Citrus maxima). This peptidase differs in specificity and in other properties from the known carboxypeptidases A (ref. 1) and B (ref. 2) of the pancreas and from the catheptic Carboxypeptidase of brain3. This citrus peptidase or enzyme mixture, referred to for short as Carboxypeptidase C, is the first Carboxypeptidase to be demonstrated in vegetable tissue. CarboxypeptidaseC belongs to the catheptic peptidases—a group which, if we extend and re-define the term ‘cathep-sin’, can also be said to include the glycyl–glycine–dipeptidase4 and leucinaminopeptidase5 found in leaves.
Similar content being viewed by others
Article PDF
References
Putnam, R. W., and Neurath, H., J. Biol. Chem., 166, 603 (1946). Smith, E. L., Adv. Enzymol., 12, 233 (1951). Neurath, H., The Enzymes, 4, 11 (Academic Press, New York and London, 1960).
Folk, J. E., and Gladner, J. A., J. Biol. Chem., 231, 379 (1958).
Greenbaum, L. M., and Sherman, R., J. Biol. Chem., 237, 1082 (1962).
Ambros, O., and Harteneck, Z., Z. Physiol. Chem., 184, 93 (1929). Linderstrøm-Lang, K., and Holter, H., ibid., 204, 15 (1932). Mounfield, J. M., Biochem. J., 30, 549, 1778 (1936).
Linderstrøm-Lang, K., and Sato, M., Z. Physiol. Chem., 184, 83 (1929). Berger, J., and Johnson, M. J., J. Biol. Chem., 130, 655 (1939).
Measured: hydrolysis of Z·Leu-Phe·OH.
C1 proteolytic coefficient, k1 = rate constant (min−1), first-order reaction; substrate conc. 0.001 M, pH. 5.3, 30° C, enzyme cone, fraction E1 = 0.2 or 1 mg protein N/c.c.
Protein concentration measured by Folin-Lowry method(J. Biol. Chem., 193, 265 (1951)).
Smith, E. L., and Hanson, H. T., J. Biol. Chem., 179, 803 (1949).
Harris, J. J., and Roos, P., Biochem. J., 71, 434 (1959).
Jansen, E. F., Jang, R., and McDonnell, L. R., Arch. Biochem. Biophys., 15, 415 (1947). Jansen, E. F., Nutting, M. D. F., and Balls, A. K., J. Biol. Chem., 175, 975 (1948).
There are also other major differences between acetylesterase and Carboxypeptidase C (pH optimum, stability, behaviour during fractionation).
Author information
Authors and Affiliations
Rights and permissions
About this article
Cite this article
ZUBER, H. Purification and Properties of a New Carboxypeptidase from Citrus Fruit. Nature 201, 613 (1964). https://doi.org/10.1038/201613a0
Issue Date:
DOI: https://doi.org/10.1038/201613a0
This article is cited by
-
Aspartat-Proteinasen in Weizenmehl
Zeitschrift f�r Lebensmittel-Untersuchung und -Forschung (1993)
-
Proteinase activity in potato plants
Planta (1978)
-
New Enzymatic Route for the Inactivation of Angiotensin
Nature (1968)
-
Lysosomes of root tip cells in corn seedlings
Planta (1968)
Comments
By submitting a comment you agree to abide by our Terms and Community Guidelines. If you find something abusive or that does not comply with our terms or guidelines please flag it as inappropriate.