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首页> 外文期刊>Cell biology international. >CHARACTERIZATION OF TWO HUMAN cAMP-SPECIFIC FHOSPHODIESTERASE SUBTYPES EXPRESSED M BACULOVIRUSINFECTED INSECT CELLS.
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CHARACTERIZATION OF TWO HUMAN cAMP-SPECIFIC FHOSPHODIESTERASE SUBTYPES EXPRESSED M BACULOVIRUSINFECTED INSECT CELLS.

机译：表征了两种人营地特异的磷酸二酯酶亚型的表达，这些亚型表达了M杆状病毒感染的昆虫细胞。

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摘要

Recombinant baculoviruses were constructed to express cDNAs encoding two distinct subtypes of human cAMP-spedficphosphodiesterase (HPDE4A andhPDE4B). Infection of Spodoptera frugiperda insect cells with the appropriate recombinant baculoviruses resulted in high level production of biologically-active protein as measured by enzymatic activity and immunoblotting using subtype-specific anti-hPDE4 antisera. Both recombinant proteins showed catalytic activity with a low K_m (approx 3 muM)for cAMP (with nocGMP hydrofyzing activity) and were inhibited by R-rolipram with apparent K/s of 0.38 and 0.25 muM, respectively. The recombinant enzymes also contained saturable, stereoselective and high-affinity rolipram-binding sites (K_d approx 2 nM). Thus, insectcell-derived hPDE4s possess kinetic properties analogous to native enzymes as well as to recombinant enzymes produced in yeast.
机译：构建重组杆状病毒以表达编码人cAMP-spedficphosphodiesterase（HPDE4A和hPDE4B）两种不同亚型的cDNA。用适当的重组杆状病毒感染斜纹夜蛾昆虫细胞可产生高水平的生物活性蛋白，这是通过酶促活性和使用亚型特异性抗hPDE4抗血清的免疫印迹法测得的。两种重组蛋白均显示出对cAMP具有低K_m（约3μM）的催化活性（具有nocGMP水解活性），并被R-咯利普兰抑制，表观K / s分别为0.38和0.25μM。重组酶还包含可饱和的，立体选择性的和高亲和力的利利普兰结合位点（K_d约2nM）。因此，昆虫细胞衍生的hPDE4s具有类似于天然酶以及酵母中产生的重组酶的动力学特性。

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