Phosphoprotein phosphatase, a new enzyme from the frog egg.
نویسنده
چکیده
In the nutrition of the young, the r&e 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.
منابع مشابه
The intracellular location of phosphoprotein phosphatase activity.
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Entry into mitosis depends on the activity of cyclin-dependent kinases (CDKs). Conversely, exit from mitosis occurs when mitotic cyclins are degraded, thereby extinguishing CDK activity. Exit from mitosis must also require mitotic phosphoproteins to revert to their interphase hypophosphorylated forms, but there is a controversy about which phosphatase(s) is/are responsible for dephosphorylating...
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In a previous communication (Li, H.-C., Hsiao, K.-J., and Chan, W. W. S. (1978) Eur. J. Biochem 84,215-225) we reported the purification of a divalent cation-independent, nonspecific phosphoprotein phosphatase (phosphatase S, M, = 35,000) from canine cardiac muscle to apparent homogeneity. It was found that the homogeneous enzyme preparation exhibited significant activity toward p-nitrophenyl p...
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ورودعنوان ژورنال:
- The Journal of biological chemistry
دوره 165 2 شماره
صفحات -
تاریخ انتشار 1946