Hostname: page-component-586b7cd67f-gb8f7 Total loading time: 0 Render date: 2024-11-27T11:52:57.553Z Has data issue: false hasContentIssue false
  • English
  • Français

632. Reactivation of milk phosphatase following heat treatment: IV. The influence of certain metallic ions

Published online by Cambridge University Press:  01 June 2009

R. C. Wright  and
J. Tramer
R. C. Wright
Affiliation:
United Dairies Research Laboratories, Wood Lane, London, W. 12
J. Tramer
Affiliation:
United Dairies Research Laboratories, Wood Lane, London, W. 12
Get access Rights & Permissions [Opens in a new window]

Extract

1. Reactivation of alkaline milk phosphatase is affected by the presence of ions, Mg2+, Zn2+ and Mn2+ being activating and Cu2+, Ni2+ and Co2+ being inhibitory.

2. Cu2+ will inhibit reactivation induced by Mg2+, but has no effect upon Zn2+-induced reactivation.

3. Using washed cream, either alone or in admixture with boiled whey treated with cationic resin, reactivation occurs in the presence of added Mg2+, but not when Zn2+ is added.

4. Experiments with EDTA. confirm that metallic ions play a part both in alkaline phosphatase activity and in reactivation.

5. It is suggested that either Mg2+ or Zn2+ or both play a part in reactivation.

Type
Original Articles
Information
Journal of Dairy Research , Volume 23 , Issue 2 , June 1956 , pp. 248 - 256
Copyright
Copyright © Proprietors of Journal of Dairy Research 1956

Access options

Get access to the full version of this content by using one of the access options below. (Log in options will check for institutional or personal access. Content may require purchase if you do not have access.)

References

REFERENCES

(1)Wright, R. C. & Tramer, J. (1953). J. Dairy Res. 20, 258.CrossRefGoogle Scholar
(2)Fuchs, A. (1953). XIIIth Int. Dairy Congr. 3, 1018.Google Scholar
(3)Wright, R. C. & Tramer, J. (1953). J. Dairy Res. 20, 177.CrossRefGoogle Scholar
(4)Massart, L. & Vandendriessche, L. (1945). Enzymologia, 11, 261.Google Scholar
(5)Kannan, A. & Basu, K. P. (1949). Indian J. Dairy Sci. 2, 51.Google Scholar
(6)Kelly, E. (1942). Dairy Sci. Abstr. 4, 1, 41.Google Scholar
(7)Anagnostopoulos, M. C. (1953). Bull. Soc. Chim. biol., Paris, 35, 554.Google Scholar
(8)Cloetens, R. (1944). Arch. int. Pharmacodyn. 69, 386.Google Scholar
(9)Hove, E., Elvehjem, C. A. & Hart, E. B. (1940). J. biol. Chem. 134, 425.CrossRefGoogle Scholar
(10)Abul-Fadl, M. A. M. & King, E. J. (1949). Biochem. J. 44, 435.CrossRefGoogle Scholar
(11)Morton, R. K. (1955). Biochem. J. 60, 573.CrossRefGoogle Scholar