Abteilung Cytologie des Pflanzenphysiologischen Instituts der Universität, Untere Karspüle 2, D-3400, Göttingen, Federal Republic of Germany.
Planta. 1985 May;164(2):287-94. doi: 10.1007/BF00396094.
The enzyme prolyl hydroxylase which is responsible for the hydroxylation of peptidyl proline has been investigated in extracts of maize roots. The optimum conditions under which this enzyme can be assayed have been determined using both a colorometric and a radiochemical assay. The enzyme has certain features in common with vertebrate prolyl hydroxylase (pH optimum, requirement for ferrous ion, inhibition by tricine and phosphate buffers, stimulation by bovine serum albumin) but prefers poly-L-proline to collagenous substrates. Centrifugation studies shows that the enzyme is mainly membrane-bound and is primarily localized in the endoplasmic reticulum, although the presence of small amounts in the Golgi apparatus cannot be ruled out.
负责肽基脯氨酸羟基化的脯氨酰羟化酶已在玉米根提取物中进行了研究。已使用比色法和放射化学分析法确定了可测定该酶的最佳条件。该酶与脊椎动物脯氨酰羟化酶有某些共同特征（最适pH值、对亚铁离子的需求、被三羟甲基氨基甲烷和磷酸盐缓冲液抑制、被牛血清白蛋白刺激），但比起胶原底物，它更喜欢聚-L-脯氨酸。离心研究表明，该酶主要与膜结合，主要定位于内质网，不过也不能排除在高尔基体中有少量存在。
