韭菜凝集素的纯化及部分性质的研究

用葡聚糖凝胶柱层析法从韭菜的叶片组织分离出一种对新鲜兔红细胞有强烈凝集作用的凝集素，ＰＡＧＥ鉴定和高碘酸－Ｓｃｈｉｆｆ试剂反应均显单一条带。ＳＤＳ－ＰＡＧＥ分析表明该凝集素含有３个亚基，其相对分子质量分别约为３１０００、２４０００和２１０００。韭菜凝集素具有一定的热稳定性，在酸、碱处理中该凝集素对碱处理较酸处理稳定，氨基酸组成分析表明韭菜凝集素含有１４种氨基酸，其中半胱氨酸含量较高。     

生物活性物质—芦荟的抗炎,愈合活性

本文主要介绍具有生物活性的天然产物.文中以药用植物芦荟为例,通过具体的实验结果,阐明了它的抗炎与愈合活性及其机理.     

海芋凝集素的理化性质鉴定

采用葡聚糖凝胶１００（ＳｅｐｈａｄｅｘＧ－１００）从天南星科植物海芋（Ａｌｏｃａｓｉａｏｄｏｒａ（Ｒｏｘｂ）Ｃ．Ｋｏｃｈ）中分离出了一种凝集素（简称ＡＯＬ）．ＡＯＬ对兔血有较强的凝集效果,而对各类型人血的凝集活力较弱,在３种糖蛋白中,猪甲状腺球蛋白对ＡＯＬ的凝血活力抑制最强;ＡＯＬ对培养人外周血白细胞的转化率高达７９％,超过对照ＰＨＡ的转化率;用ＳｅｐｈａｄｅｘＧ－２００柱测得ＡＯＬ的相对分子质量为３１５００;用癌细胞体外培养的方法证明了ＡＯＬ对肺腺癌细胞株Ｐ１８具有较强的直接杀伤能力．此外还发现ＡＯＬ对温度（８０℃以下）、变性剂（盐酸胍和脲）有较高的稳定性,在ｐＨ６～１０的范围内相当稳定．     

金属离子和变性条件对野花生豆凝集素活性和构象的影响

野花生豆凝集素在pH7．0和pH5．0缓冲体系中，用EDTA去除其金属离子，CML凝血活性下降．Ca^2 、Mg^2 、Mn^2 、Zn^2 可使去除金属离子CML活性基本恢复到天然水平，表明这些二价金属离子为CML活性所必需．研究不同温度和不同浓度盐酸胍条件下CML的圆二色谱、荧光光谱及其凝血活性的变化，结果表明CML含有较多β-折叠，具有较强的抗变性能力；脲变性的时间扫描荧光光谱证实了CML变性过程的阶段性。     

凝集素的分离纯化、基因克隆及功能研究进展

凝集素(lectin)研究近年来发展迅速，尤其在植物基因工程中，植物外源凝集素基因越来越受到重视。本文从凝集素的分离纯化、基因克隆、理化性质和功能等方面进行了综述。此外还讨论了凝集素基因在植物基因工程中的应用。     

小鼠表皮发育期间蓖麻凝集素受体的定位

采用酶标凝集素技术，在光镜水平对小鼠表皮发育期间蓖麻凝集素的受体进行定位，结果表明；在胚胎期间周皮细胞和角质层以及基膜中均有Ｇａｌ残基分布；在表皮中间层，毛根原基处无Ｇａｌ，在眼睑和眼睑缘处也无Ｇａｌ分布，Ｇａｌ可能参与表皮的角质化和基膜组建，与周皮在胚胎期发挥正常功能有关。     

不同海藻凝集素对鲤免疫活性物的诱导作用

以条斑紫菜（Porphyra yezaensis）和裙带菜（Undaria pinnatifida）的凝集素作为免疫增强剂，来研究它对鲤免疫活性的诱导作用．实验结果表明，投喂和灌喂凝集素后，鲤血清中凝集素、超氧化物歧化酶（SOD）、过氧化氢酶（CAT）、溶菌酶活性与对照组相比都有提高，其中投喂条斑紫菜凝集素组比投喂对照组依次提高3．0倍、0．8倍、3．9倍、1.0倍；投喂裙带菜凝集素组比投喂对照组依次提高1.0倍、0．4倍、3．0倍、0．7倍，灌喂裙带菜凝集素组比灌喂对照组依次提高3．0倍、0．3倍、1．8倍；灌喂条斑紫菜凝集素组比灌喂对照组依次提高3.0倍、0．7倍．由此可看出：两种凝集素都可以作为一种免疫添加剂激活鲤的免疫系统，对鲤的非特异性免疫功能具有明显的增强作用．其中投喂条斑紫菜的效果更好．     

文蛤(Meretrix Meretrix)凝集素(MML)的初步研究——Ⅰ.MML在文蛤体内的分布及纯化

在文蛤(Meretrix Meretrix)体内具有血球凝集活性的凝集素(简称MML),经实验证实仅分布于文蛤外套腔液中。向外套腔液中加入固体硫酸铵达40％时,可使99％的MML沉淀。用不同饱和度的硫酸铵溶液依次对上述沉淀进行抽提,得到MML粗制品溶液,其比活比原始外套腔液提高了约9.95倍,总活力回收达48％。最后用自制的人血浆糖蛋白一Sepharose 4 B亲合层析柱可将上述MML粗制品的比活再提高400多倍。结果与原始外套腔液比较,MML终产品的比活总共提高了4313倍,总活力回收达44.8％,在电泳鉴定时显示出单一的区带。     

Role of <Emphasis Type="Italic">N</Emphasis>-linked polymannose oligosaccharides in targeting glycoproteins for endoplasmic reticulum-associated degradation

Misfolded or incompletely assembled multisubunit glycoproteins undergo endoplasmic reticulum-associated degradation (ERAD) regulated in large measure by their N-linked polymannose oligosaccharides. In this quality control system lectin interaction with Glc₃Man₉GlcNAc₂ glycans after trimming with endoplasmic reticulum (ER) -glucosidases and -mannosidases sorts out persistently unfolded glycoproteins for N-deglycosylation and proteolytic degradation. Monoglucosylated (Glc₁Man₉GlcNAc₂) glycoproteins take part in the calnexin/calreticulin glucosylation-deglucosylation cycle, while the Man₈GlcNAc₂ isomer B product of ER mannosidase I interacts with EDEM. Proteasomal degradation requires retrotranslocation into the cytosol through a Sec61 channel and deglycosylation by peptide: N-glycosidase (PNGase); in alternate models both PNGase and proteasomes may be either free in the cytosol or ER membrane-imbedded/attached. Numerous proteins appear to undergo nonproteasomal degradation in which deglycosylation and proteolysis take place in the ER lumen. The released free oligosaccharides (OS) are transported to the cytosol as OS-GlcNAc₂ along with similar components produced by the hydrolytic action of the oligosaccharyltransferase, where they together with OS from the proteasomal pathway are trimmed to Man₅GlcNAc₁ by the action of cytosolic endo--N-acetylglucosaminidase and -mannosidase before entering the lysosomes. Some misfolded glycoproteins can recycle between the ER, intermediate and Golgi compartments, where they are further processed before ERAD. Moreover, properly folded glycoproteins with mannose-trimmed glycans can be deglucosylated in the Golgi by endomannosidase, thereby releasing calreticulin and permitting formation of complex OS. A number of regulatory controls have been described, including the glucosidase-glucosyltransferase shuttle, which controls the level of Glc₃Man₉GlcNAc₂-P-P-Dol, and the unfolded protein response, which enhances synthesis of components of the quality control system.Received 26 January 2004; accepted 25 February 2004