Morozov V I, Tsyplenkov P V, Kokryakov V N, Volkov K N, Vinogradova N A
Department of Biochemistry, Institute of Physical Culture, St. Petersburg, Russia.
Biochemistry (Mosc). 1997 Jun;62(6):623-30.
Myeloperoxidase (MPO) was isolated from rat peritoneal leukocytes with a yield of 51% and A430/A280 = 0.75 - 0.80, and its physicochemical properties were studied. The molecular weight of the MPO is about 150 kD. The MPO was assayed for amino acid content. We used substrate mixture containing phenol, 4-aminoantipyrine, and H2O2 to detect 10(-10) M of the enzyme. The MPO was localized in rat blood neutrophils using polyclonal anti-MPO antibodies and secondary fluorescein isothiocyanate-labeled antibodies. Immunofluorimetric assay (IFMA) was developed for quantitative measurement of the MPO. The MPO and leukocytes can iodinate BSA using NaI or thyroxine as the source of iodine.
从大鼠腹腔白细胞中分离出髓过氧化物酶（MPO），产率为51%，A430/A280 = 0.75 - 0.80，并对其理化性质进行了研究。MPO的分子量约为150 kD。对MPO的氨基酸含量进行了测定。我们使用含有苯酚、4-氨基安替比林和H2O2的底物混合物来检测10(-10) M的该酶。使用多克隆抗MPO抗体和异硫氰酸荧光素标记的二抗将MPO定位在大鼠血液中性粒细胞中。开发了免疫荧光测定法（IFMA）用于MPO的定量测量。MPO和白细胞可以使用NaI或甲状腺素作为碘源对牛血清白蛋白进行碘化。
