不同生境中猴腿蹄盖蕨种群调查

猴腿蹄盖蕨〔Athyrium multidentatum(Dol.)Ch ing〕是一种食药兼用型植物,为了合理的开发利用,在吉林省东南部山区临江市境内,调查分析了其分布的5个典型群落,并测量株高、冠幅、密度和含水率。结果表明:猴腿蹄盖蕨的生态适宜性较广,不同群落条件下株高、冠幅、密度差异较大,水分和光照强度是影响其生长发育和繁殖的主要生态因子,适当的强光照和高湿度条件有利于猴腿蹄盖蕨的有性繁殖和生长发育,针阔混交林林缘和白桦次生林林窗群落条件最适宜猴腿蹄盖蕨种群的发展。环境条件的差异对含水率的影响较小。通过探讨适合种群生长发育的环境条件,为引种驯化提供科学依据。     

The glutathione thiol-disulfide status in the sea urchin egg during fertilization and the first cell division cycle

The intracellular levels of GSH, GSSG, and protein-glutathione disulfide (protein-SSG) have been measured in the eggs and developing embryos of the sea urchins Lytechinus pictus and Strongylocentrotus purpuratus. Total cellular glutathione is maintained in a very highly reduced state during these initial stages of development. Thus for unfertilized eggs of L. pictus the results (μmol/g dry weight) were 11 ± 1 for GSH, 0.02 ± 0.01 for GSSG, and 0.07 ± 0.02 for protein-SSG. No significant change in these values was observed upon fertilization of the eggs or during the first cell division cycle. The values obtained with S. purpuratus were somewhat greater, but were also found to exhibit no significant variations upon fertilization or cell division. These observations indicates that changes in the total cellular glutathione thiol-disulfide status are not involved in the control mechanisms which operate during fertilization or the first cell division cycle in the sea urchin egg.     

Glycosylation of endogenous proteins through dolichol derivatives in reticulocyte plasma membranes

It has been found that rabbit reticulocyte plasma membranes contain the enzymatic activities responsible for the synthesis of all the polyprenol-bound sugars that are intermediates in the glycosylation of proteins. The final reaction in which an oligosaccharide is transferred from a dolichol pyrophosphate derivative to an endogenous protein was detected in reticulocyte but not in erythrocyte plasma membranes.     

Differential effects of thyrotropin on various glycosyltransferases in porcine thyroid cells

Porcine thyroid cells were cultured with or without thyrotropin for 9 days. It is known that the hormone enhances the synthesis of thyroglobulin, with an increase in the content and stability of its m-RNA. We show in the present work that thyrotropin also stimulates a number of glycosyltransferases diversely situated along the process of N-glycosylation. The most increased was oligosaccharyltransferase, responsible for attachment to nascent peptides of preformed core carbohydrate sequences. The relatively low activity level of oligosaccharyltransferase and its preferential responsiveness to thyrotropin supports the possibility of a regulation point at this enzyme.