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Phosphoprotein phosphatase, a new enzyme from the frog egg

Harris, Daniel L. (1946) Phosphoprotein phosphatase, a new enzyme from the frog egg. Journal of Biological Chemistry, 165 (2). pp. 541-550. ISSN 0021-9258. http://resolver.caltech.edu/CaltechAUTHORS:HARjbc46

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Abstract

In the nutrition of the young, the role of phosphoproteins is, without doubt, an important one. As casein in milk, or as the yellow yolk of many vertebrate and invertebrate eggs, phosphoprotein occurs in substantial quantities. In the frog egg, for example, the yolk platelets occupy almost half the volume of the cell. According to McClendon (5), the yolk of the frog egg consists of phosphoprotein bound to lipide; thus the platelets are a ready source of protein, lipide, and phosphorus. And yet, in spite of the obvious importance of phosphoprotein, little information is available about the manner of its utilization by the developing embryo. It has been assumed that ordinary proteolytic enzymes degrade the protein, and that ordinary phosphomonoesterases split the phosphate from phosphopeptone or from phosphoserine. In the course of an investigation of the distribution of enzymes in the frog egg, a new enzyme (or enzymes) was discovered which is apparently capable of splitting inorganic phosphate from the intact protein molecule. It is the purpose of this paper to present the experiments which led to this conclusion.


Item Type:Article
Additional Information:Copyright © 1946 by the American Society of Biological Chemists (Received for public&ion, June 7, 1946) I am grateful for helpful discussions with the late Dr. Carl L. A. Schmidt and Dr. D. M. Greenberg, and for the cooperation of Miss Mary Cregar who assisted me in some of these experiments. [D.L.H. was a] National Research Council Fellow in Zoology, 1942-43.
Record Number:CaltechAUTHORS:HARjbc46
Persistent URL:http://resolver.caltech.edu/CaltechAUTHORS:HARjbc46
Alternative URL:http://www.jbc.org/content/vol165/issue2/index.shtml
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ID Code:5842
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Deposited On:04 Nov 2006
Last Modified:26 Dec 2012 09:15

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