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We have studied the turnover and synthesis of purine nucleoside phosphorylase by using a polyclonal rabbit antiserum to this protein. The turnover of purine nucleoside phosphorylase was studied in the B lymphoblast cell, WI-L2, by specific immunoprecipitation of [3H]leucine-labeled proteins. The half-lives for total protein and purine nucleoside phosphorylase were 14.5 and 14.1 hr, respectively. For cells cultured in the presence of inosine the half-life of purine nucleoside phosphorylase was reduced to 11.2 hr. The synthesis of purine nucleoside phosphorylase was analyzed during phytohemagglutinin-stimulated T cell transformation by pulse labeling cells with [35S]methionine. Purine nucleoside phosphorylase synthesis increased greater than 10-fold during the first 12 hr of transformation and continued to a maximum of 30-fold. The relative rate of purine nucleoside phosphorylase labeled to total proteins was 0.04% in unstimulated T cells and increased to 0.18% 12 hr after stimulation. These studies identify some preferential synthesis of purine nucleoside phosphorylase during the early stages of T cell transformation.
K Neote, and
E Kwan, and
F F Snyder
January 1978,
Methods in enzymology,
K Neote, and
E Kwan, and
F F Snyder
January 2013,
Biomeditsinskaia khimiia,
K Neote, and
E Kwan, and
F F Snyder
June 1979,
Nihon rinsho. Japanese journal of clinical medicine,
K Neote, and
E Kwan, and
F F Snyder
November 2004,
Nihon rinsho. Japanese journal of clinical medicine,
K Neote, and
E Kwan, and
F F Snyder
January 2000,
Ryoikibetsu shokogun shirizu,
K Neote, and
E Kwan, and
F F Snyder
January 2003,
Nihon rinsho. Japanese journal of clinical medicine,
K Neote, and
E Kwan, and
F F Snyder
January 1991,
Immunodeficiency reviews,
K Neote, and
E Kwan, and
F F Snyder
December 1996,
Nihon rinsho. Japanese journal of clinical medicine,
K Neote, and
E Kwan, and
F F Snyder
July 1978,
Cell,
K Neote, and
E Kwan, and
F F Snyder
November 2003,
Journal of medicinal chemistry,
