从大鼠唾液腺中纯化无机焦磷酸酶。
Purification of inorganic pyrophosphatase from rat salivary glands.
作者信息
Koskowska-Dziadowicz M, Ochman M, Szymczyk T
机构信息
Department of Biochemistry, Institute of Biopharmacy, Medical Academy in Warsaw, Poland.
出版信息
Acta Biochim Pol. 1990;37(3):345-58.
Inorganic pyrophosphatase [EC 3.6.1.1] isolated from rat sublingual and submandibular glands was purified 2300-fold and 2600-fold, respectively. The purified enzymatic preparations separated on electrophoresis into two protein bands, of which only one showed the pyrophosphatase activity. Inorganic pyrophosphatase from rat salivary glands is a monomeric anionic protein, its isoelectric point is 5.42 and 4.90 for the sublingual and submandibular glands, respectively.
从大鼠舌下腺和下颌下腺分离出的无机焦磷酸酶[EC 3.6.1.1]分别被纯化了2300倍和2600倍。纯化后的酶制剂在电泳中分离成两条蛋白带，其中只有一条显示出焦磷酸酶活性。大鼠唾液腺的无机焦磷酸酶是一种单体阴离子蛋白，舌下腺和下颌下腺的无机焦磷酸酶的等电点分别为5.42和4.90。
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