全麻剂作用下Ca~(2 )诱导膜融合的研究

全麻剂通过干扰膜的结构与功能而起作用，研究了四种全麻剂（氯仿、乙醚、乙醇及辛醇）对３ｍｍｏｌＣａ２＋诱导融合影响用ＰＳ：ＤＭＰＣ：Ｃｈｏｌｅｓｔｅｒｏｌ＝５：３：２的人工膜脂质体进行实验，脂质体融合用荧光共振能量转移监测，初步实验表明：在临床浓度范围内，氯仿，乙酸及辛醇能轻微地抑制膜融合，而乙醇在临床浓度附近能促进膜融合，并且随着乙醇浓度的提高其促融合效应变得十分明显，这可能是乙醇分子的极性及通过氢键与磷脂头缔结，并取代部份结构水，减弱水化排斥力而促使膜融合。     

Lipid transport pathways in mammalian cells

Summary A major deficit in our understanding of membrane biogenesis in eukaryotes is the definition of mechanisms by which the lipid constituents of cell membranes are transported from their sites of intracellular synthesis to the multiplicity of membranes that constitute a typical cell. A variety of approaches have been used to examine the transport of lipids to different organelles. In many cases the development of new methods has been necessary to study the problem. These methods include cytological examination of cells labeled with fluorescent lipid analogs, improved methods of subcellular fractionation, in situ enzymology that demonstrates lipid translocation by changes in lipid structure, and cell-free reconstitution with isolated organelles. Several general patterns of lipid transport have emerged but there does not appear to be a unifying mechanism by which lipids move among different organelles. Significant evidence now exists for vesicular and metabolic energy-dependent mechanisms as well as mechanisms that are clearly independent of cellular ATP content.     

固体颗粒诱导双亲分子自组装形成颗粒@囊泡复合体

固体颗粒可诱导两亲分子自组装形成囊泡及颗粒@囊泡复合体。该复合体在支撑双层膜的构筑、悬浮体的稳定、特殊结构材料的制备及药物输送-控释体系的构建等方面具有重要的应用前景,本文对此进行了综述。     

Novel Chitosan-based Biomaterials

1 Introduction Chitosan with two long side chains of N-alkyl group is an important amphiphilic material, which has potential application in tissue engineering and drug delivery system. In this paper the amphiphilic N, N-dilauryl chitosan has been prepared by the phase transfer catalysis. The π-A isotherms of the products were measured in order to find some fundamental data for making self-assembled vesicles out of this kind of material. The LB film experiment indicates that N, N-dilauryl …     

The toxicity of twoBacillus thuringiensis δ-endotoxins to gypsy moth larvae is inversely related to the affinity of binding sites on midgut brush border membranes for the toxins

Summary The-endotoxin fromBacillus thuringiensis subspecieskurstaki strain HD1-9 is almost 400 times more potent than the-endotoxin from strain HD-73 as a gypsy moth larvicide. The two-endotoxins compete for a high-affinity binding site on the brush border membrane of larval gypsy moth midguts. The affinity for the-endotoxin from strain HD-73 is much greater than the affinity for the-endotoxin from strain HD1-9.     

Gamma-aminobutyric acid uptake by rat kidney brush-border membrane vesicles

Summary Brush-border membrane vesicles (BBMV) from rat kidney cortex possessed two uptake systems for -aminobutyric acid (GABA), a high affinity system (Km=10.9 M) and a low affinity system (Km=1203 M). Both uptake systems were inhibited by p-hydroxymercuribenzoic acid and ouabain, and by the action of neuraminidase, whereas the GABA analogs nipecotic acid, -alanine, 2,4-diaminobutyric acid and 4,5,6,7-tetrahydroisoxazolo-[4,5c]-pyridin-3-ol had no effect on the GABA uptake activity. The BBMW uptake systems were clearly different from the GABA transport systems present in brain tissue.     

Spermine protects protein kinase C from phospholipid-induced inactivation

Phosphatidylserine (PS), an activator of protein kinase C (PKC) in the assay of protein phosphorylation, inhibited this enzyme in a time-dependent manner following preincubation in the absence of Ca²⁺. The phospholipid-induced inactivation of kinase activity was dependent on the PS content and on the charge density of liposomes. This inactivation of PKC could be reduced, but not completely eliminated, by addition of Ca²⁺. In the present work the effect of a naturally occurring polyamine (spermine) on the PS-induced inactivation of PKC was investigated. The presence of spermine during preincubation without Ca²⁺ was effective in suppressing the PS-induced inactivation of PKC over the period (20 min) required for PS to inhibit the enzyme by 95%. PKC exists in two membrane-bound states: a reversible one which can be dissociated by Ca²⁺ chelators (membrane-associated form) and an irreversible one which is chelator-stable (membrane-inserted form). Gel filtration experiments on the PKC-PS complex formed in the presence of Ca²⁺ indicated that less insertion of enzyme into liposomes occurred in the presence of spermine and that the kinase activity of the reversibly membrane-associated PKC was protected from PS inactivation.     

Colorimetric detection of glucose and an assay for acetylcholinesterase with amine-terminated polydiacetylene vesicles

The colorimetric response of amine-terminated polydiacetylene (PDA) vesicles was initially demonstrated by varying the pH of the solution. Convenient colorimetric methods to detect glucose and acetylcholinesterase (AChE) activity were successfully established using amine-terminated PDA vesicles by taking advantage of the following features: (1) the amine-terminated PDA vesicles undergo a colorimetric transition as the pH of the solution changes; (2) glucose can be oxidized to gluconic acid in the presence of glucose oxidase; and (3) AChE catalyzes the hydrolysis of acetylcholine to acetic acid. The visual detection of glucose levels and AChE activity showed good selectivity and acceptable sensitivity. The detection limit of glucose was ~2.5 μmol/L and the level of AChE activity was assayed as low as 10.0 mU/mL. Moreover, the amine-terminated PDA vesicles can be used for screening the activity of inhibitors against AChE.     

A role for the hinge/ear domain of the β chains in the incorporation of AP complexes into clathrin-coated pits and coated vesicles

The clathrin-associated adaptor protein (AP) complexes drive the polymerization of clathrin in coated pits to form coated vesicles. It has previously been shown that the carboxyl-terminal hinge/ear domain of the β2 chain contains a binding site for clathrin and that removal of this domain from APs or from isolated β2 chains abrogates their ability to form clathrin coats in vitro. We show here that the hinge/ear domain is necessary for efficient incorporation of AP complexes into coated pits and coated vesicles in cells, a result that is consistent with the view that the β chains indeed provide an important interaction between the AP complexes and clathrin. Received 7 April 1997; received after revision 22 May 1997; accepted 28 May 1997     

Effect of fatty acids on poly-amine contents and Na+/H+antiport activity in PM vesi-cles isolated from roots ofbarley under salt stress

With 200 mmol/L NaCI treatment on barleycultivar "Jian 4" (Hordeum vulgare L. cv. J4) seedlings for6 d, the contents of covalently and noncovalently conjugatedpolyamines (PAs) and activities of H+-ATPase in plasmamembrane (PM) vesicles isolated from the roots decreasedremarkably. Moreover, the activity of Na+/H+ antiport wasdetected first in PM vesicles. The results showed that thedecrease in the contents of membrane phospholipid, nonco-valently conjugated PAs and activity of H+-ATPase caused byNaCl could be restored partially by application of 1 mmol/Lstearic acid (C16:0) and linoleic acid (C18:2), and C18:2 wasmore effective than C16:0. In addition, a reduction in the con-tents of covalently conjugated PAs was only reversed par-tially in the presence of C18:2. Furthermore, Na+/H+ antiportactivity was strengthened by exogenous C16:0 and C18:2, andC18a was more effective than C16:0. The correlative analysissuggested that, after application of C16:0 and C18:2 under saltstress, there was a significant positive correlation existingamong phospholipid content, noncovalently conjugated PAlevels, H+-ATPase activities and Na+/H+ antiport activities,indicating that one of the mitigative mechanisms of exoge-nous fatty acids on salt injury was to improve membranephospholipid and PA contents, leading to an enhance inmembrane integrity and a change in charge status of PMvesicles, so the activity of membrane-associated enzymeH+-ATPase was increased and synthesis of Na+/H+ antiportprotein was activated.