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首页> 外文期刊>Journal of Plant Physiology >Purification and characterization of hordolisin, a subtilisin-like serineendoprotease from barley
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Purification and characterization of hordolisin, a subtilisin-like serineendoprotease from barley

机译：大麦中一种枯草杆菌蛋白酶样丝氨酸内切蛋白酶Hordolisin的纯化和表征

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摘要

A protease was purified from green barley (Hordeum vulgare L.) malt with an apparent molecular mass or 74 kD and a pI of 6.9. Activity was assayed using an internally quenched fluorogenic peptide substrate, and the inhibitor profile indicated that the catalytic site contained a serine residue. This was confirmed by labelling with [C-14]-diisopropyl fluorophosphate. The N-terminal amino acid sequence of the purified protease was homologous to plant subtilisin-like serine endoproteases, such as cucumisin. The barley protease (trivial name hordolisin) had a pH optimum of 6 and tvas stable up to 60 degrees C. The substrate specificity of hordolisin was determined from P-4 to P-3' using a series of internally quenched fluorogenic peptide substrates. Hordolisin was similar to Savinase and subtilisin BPN', except that Ala was better accepted at P-1, and Arg was preferred at P-1'. Hordolisin does not appear to be important in the degradation of the hordein storage proteins during barley grain germination.
机译：从表观分子量或74kD和pI为6.9的绿色大麦（Hordeum vulgare L.）麦芽中纯化蛋白酶。使用内部淬灭的荧光肽底物测定活性，并且抑制剂谱表明催化位点含有丝氨酸残基。通过用[C-14]-氟磷酸二异丙酯标记可以确认这一点。纯化的蛋白酶的N-末端氨基酸序列与植物枯草杆菌蛋白酶样丝氨酸内切蛋白酶，例如姜黄素是同源的。大麦蛋白酶（俗称hordolisin）的最适pH为6，tvas稳定至60摄氏度。使用一系列内部淬灭的荧光肽底物，从P-4至P-3'确定了Hordolisin的底物特异性。 Hordolisin与Savinase和subtilisin BPN'类似，不同之处在于Ala在P-1处更易被接受，而Arg在P-1'处更易被接受。大麦籽粒萌发期间，大麦醇溶蛋白似乎对大麦醇溶蛋白贮藏蛋白的降解并不重要。

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