Denyer K, Sidebottom C, Hylton C M, Smith A M
John Innes Institute, Norwich, UK.
Plant J. 1993 Jul;4(1):191-8. doi: 10.1046/j.1365-313x.1993.04010191.x.
Developing wild-type pea embryos contain two major isoforms of starch synthase and two isoforms of starch-branching enzyme. One of the starch synthases and both starch-branching enzymes occur both in the soluble fraction and tightly bound to starch granules. The other starch synthase, which is very similar to the waxy proteins of other species, is exclusively granule-bound., It is inactive when solubilized in a native form from starch granules, but activity is recovered when the SDS-denatured protein is reconstituted from polyacrylamide gels. Evidence is presented which indicates that all of these proteins become incorporated within the structure of the granule as it grows. It is proposed that the granule-bound waxy protein is active in vivo at the granule surface, whereas the remaining proteins are active in the soluble fraction of the amyloplast. The proteins become trapped within the granule matrix as the polymers they synthesize crystallize around them, and they probably play no further part in polymer synthesis.
发育中的野生型豌豆胚胎含有两种主要的淀粉合酶同工型和两种淀粉分支酶同工型。其中一种淀粉合酶以及两种淀粉分支酶既存在于可溶部分,也紧密结合在淀粉颗粒上。另一种淀粉合酶与其他物种的蜡质蛋白非常相似,仅与颗粒结合。当以天然形式从淀粉颗粒中溶解时它没有活性,但当SDS变性蛋白从聚丙烯酰胺凝胶中重构时活性得以恢复。有证据表明,随着颗粒的生长,所有这些蛋白质都被整合到颗粒结构中。有人提出,颗粒结合的蜡质蛋白在体内颗粒表面具有活性,而其余蛋白质在造粉体的可溶部分具有活性。随着它们合成的聚合物在其周围结晶,这些蛋白质被困在颗粒基质中,并且它们可能在聚合物合成中不再发挥进一步作用。