大豆微核心种质蛋白质及脂肪含量的遗传变异

大豆是人类最重要的植物蛋白和油脂来源。提高大豆蛋白质及脂肪含量一直是大豆品质育种的重要研究方向。采用NIR检测方法,对77份大豆微核心种质进行蛋白质及脂肪含量分析,探讨微核心种质蛋白质及脂肪含量的遗传变异特性及其与主要农艺性状的相关性,为种质利用及品质育种提供依据。结果表明,蛋白质含量和脂肪含量在品种间和生态区间均存在极显著的差异,变异丰富;蛋白质含量和脂肪含量的变异幅度为40.68%~50.03%和13.81%~21.51%,平均含量为45.95%和17.42%,变异系数为4.42%和7.96%;不同生态区品种蛋白质含量为南方品种>黄淮海品种>北方品种>国外品种,脂肪含量则相反。蛋白质含量与脂肪含量呈极显著负相关(r=-0.825**),与单株粒数和单株荚数呈极显著和显著负相关(r=-0.205**,r=-0.156*),与底荚高度呈极显著正相关(r=0.240**)。主成分分析显示,4个主成分可解释82.25%信息,分别为产量构成因子、品质因子、株型因子和粒重因子。     

中国北方地区大豆主栽品种五种成分检测与分析

对中国北方黑龙江省、吉林省、内蒙古3省50种大豆主栽品种进行检测分析,分别测定了蛋白质、脂肪、植酸、总异黄酮和胰蛋白酶抑制剂的含量。通过分析不同省份大豆品种各项指标平均含量得出：黑龙江省大豆蛋白质、植酸、总黄酮平均含量最高,脂肪氧化酶含量最低;吉林省大豆脂肪平均含量最高,蛋白质、总黄酮含量最低;内蒙古大豆脂肪氧化酶平均含量最高,脂肪、植酸含量最低。对不同省份之间大豆品种各项指标平均含量进行差异性分析得出：各省份脂肪、脂肪氧化酶平均含量差异显著或极显著,蛋白质、植酸含量差异显著或不显著,总黄酮含量差异不显著。各省大豆品种之间相关性分析结果表明：蛋白含量、脂肪含量、总黄酮含量和脂肪氧化酶含量之间两两呈负相关关系,植酸含量与蛋白质含量、总黄酮含量呈正相关关系,与脂肪含量、脂肪氧化酶含量呈负相关关系。     

高效液相色谱(HPLC)技术鉴定中国南方大豆品种异黄酮主要组分

采用高效液相色谱(HPLC)技术检测中国南方六个省份的249份大豆品种异黄酮主要组分含量.结果显示大豆籽粒中可检测出6种主要的异黄酮组分,分别为大豆甙(Daidzin)、甲氧基黄豆甙原(Glycitin)、染料木甙(Genistin)、丙二酰基大豆甙(Malonyldaidzin)、丙二酰基黄豆甙原(Malonylglycitin)和丙二酰基染料木甙(Malonylgenistin).各组分中以丙二酰基(Malonyl)异黄酮组分含量最高(61.2%),且各组分间相关极显著.大豆品种间异黄酮含量变异较大,变异系数达49.6%.来自江苏省的品种海门红黄豆乙异黄酮含量最高(4932.3μg/g),品种宝应等西风含量最低(367.1μg/g).不同省份间异黄酮含量差异极显著,来自浙江省的大豆品种平均含量最高(2717.2μg/g),来自安徽省的平均含量最低(1181.8μg/g).异黄酮含量与生育期呈极显著正相关(r=0.319* * *),与百粒重呈显著正相关(r=0.132*),而与脂肪含量(r=-0.45* * *)和蛋白质含量(r=-0.136)呈负相关.     

发酵法精制大豆低聚糖的研究

研究了三种面包酵母对大豆低聚糖碳源利用的选择性。结果表明 :面包酵母C可选择性地利用蔗糖 ,而水苏糖和棉子糖的保留率大于 96 %;通过添加酵母膏 ,经过 3 6h培养 ,面包酵母C可全部利用大豆低聚糖中的蔗糖。进一步研究表明 ,以大豆乳清废糖浆为原料直接发酵再经下游处理 ,可得到蔗糖含量低于 1 3 %的精制大豆低聚糖干粉。     

利用野生大豆资源创新优质抗病大豆新种质

利用野生大豆与栽培大豆种间杂交中间材料与高产栽培大豆回交转育,创新选育出蛋白质含量45％以上,蛋脂总含量63％以上,分别抗大豆疫霉根腐病,抗大豆灰斑病,农艺性状优良的大豆创新种质资源3份。其中,龙品8802-1抗大豆疫霉根腐病兼抗大豆灰斑病,蛋白质含量45．64％,脂肪含量18．42％,蛋脂总含量64．06％;龙品01-757抗大豆灰斑病,蛋白质含量45．99％,脂肪含量19．4％,蛋脂总含量65．39％;龙品9501,中抗大豆灰斑病,蛋白质含量45．11％,脂肪含量18．32％,蛋脂总含量63．43％。研究结果表明,利用含有野生大豆血缘的种间杂交材料与高产栽培大豆回交,是拓宽大豆遗传基础,创新选育优质、抗病、农艺性状优良大豆新种质资源的有效途径。     

新收集大豆种质资源主要品质鉴定与评价

对"十五"期间新收集、保存入国家种质资源库的841份大豆种质资源的蛋白质、脂肪两个主要品质性状进行了鉴定评价.结果表明,蛋白质、脂肪含量均近似正态分布,最大频度分别出现在41.01%～ 42.00%含量范围和20.01%～21.00%含量范围.与以前收集、保存的种质资源相比,新收集种质资源的蛋白质含量呈下降趋势,而脂肪含量和蛋脂总量呈上升趋势.不同类型种质资源的品质性状比较结果表明,地方品种的蛋白质总体水平明显高于育种材料、引进种质和选育品种3种类型,引进种质的脂肪、蛋脂总量的总体水平明显高于其他3种类型.国内种质资源高蛋白质大豆占有率高于引进种质资源;引进种质资源高脂肪、高蛋白兼高油的大豆占有率高于国内种质资源.     

干旱区绿洲农田不同种植模式和秸秆管理下土壤质量评价

研究干旱区绿洲农田不同种植模式和秸秆管理下土壤有机碳及其酶活性的变化,揭示农业管理措施对土壤质量的影响,以期为干旱区农业资源高效利用及可持续发展提供理论依据.在作物种植规划区,选择新疆主要农作物棉花、小麦、玉米,设计长期连作及轮作试验.结果表明:轮作处理土壤有机碳(SOC)、微生物生物量碳、易氧化有机碳、水溶性有机碳、热水溶性有机碳含量较连作处理分别提高了3.6%~9.9%、41.8%~98.9%、3.3%~17.0%、11.1%~32.4%、4.6%~27.5%;秸秆还田处理较秸秆不还田处理分别提高了12%~35.9%、22.4%~49.7%、30.7%~51.0%、10.6%~31.9%、41.0%~96.4%.轮作处理土壤过氧化氢酶、脱氢酶、β-葡萄糖核苷酶、蔗糖酶、纤维素酶活性较连作处理分别提高了6.4%~10.9%、6.6%~18.8%、5.9%~15.3%、10.0%~27.4%、28.1%~37.5%;秸秆还田处理较-秸秆不还田处理分别提高了31.4%~47.5%、19.9%~46.6%、13.8%~20.7%、19.8%~55.6%、54.1%~70.9%.相关性分析表明,SOC及其活性组分与土壤酶活性之间有极显著的正相关关系,利用土壤活性有机碳组分和酶活性变化可有效表征农田SOC和土壤质量变化.通过因子分析综合评价得知,在干旱区农业生产中,短期连作棉花兼实施秸秆还田可提高SOC及其活性组分含量和酶活性,合理轮作可有效缓解连作障碍,使土壤质量得到进一步改善,有利于农田土壤的可持续利用.     

2002年我国大豆(Glycine max)品种及种质资源的蛋白质和脂肪含量分析

对2002年全国14个主要大豆种植省(区)的大豆品种及其种质资源的蛋白质、脂肪含量进行了分析。结果表明,种质资源的蛋白质、脂肪平均含量均高于生产用品种。其中种质资源脂肪含量的变化幅度较大,显示了在未来的育种中更强的高脂肪含量的选择优势。国内种质资源蛋白质平均含量高于国外种质资源。国外种质资源脂肪含量总体上高于国内种质资源。黄淮海生态区品种蛋白质平均含量高于北方生态区品种。新育成黄淮海区域试验品种蛋白质平均含量高于目前黄淮海生态区生产用品种。同品种异地种植,其脂肪含量有明显变化。     

水稻直链淀粉和蛋白质突变系筛选及其与主要农艺性状的关联分析

研究利用重离子辐照杂交籼稻9311创建农艺性状突变体库,使用化学方法筛选直链淀粉、蛋白质突变材料,并分析籽粒品质性状与农艺性状之间的相关性,为后续筛选直链淀粉、蛋白质突变体工作奠定基础。结果显示:在169份直链淀粉、蛋白质突变体中,直链淀粉含量变幅范围是7.64%~32.37%,其中高含量直链淀粉突变体材料有11份,低含量直链淀粉突变体材料有5份;蛋白质含量变幅范围是7.05%~13.79%,其中高蛋白突变体有34份,低蛋白突变体有3份。从169份突变体中筛选出直链淀粉、蛋白质含量都有梯度差异的突变体材料,筛选出材料的农艺性状分析结果表明:在直链淀粉、蛋白质突变体材料的农艺性状中,每穗实粒数、有效穗数、结实率和株高这四个农艺性状与籽粒品质性状间有关联,变异系数分别为37.53%、30.72%、24.70%、15.38%。相关性结果表明:直链淀粉含量和蛋白质含量呈负相关,直链淀粉含量与农艺性状呈正相关,蛋白质与农艺性状呈负相关,其中蛋白质含量和每穗实粒数、结实率呈极显著负相关,相关系数分别为-0.504、-0.592。     

山西不同生态型大豆种质资源蛋白亚基的变异

选用山西57份不同生态型大豆种质资源为材料,利用SDS-PAGE梯度电泳技术分离11S球蛋白和7S伴球蛋白各主要亚基,通过Quantity One 4.52软件得出11S和7S及其亚基的相对含量。结果表明,不同生态型大豆种质资源间同一亚基相对含量存在较大变异,其中变异系数最大的为β亚基,变异幅度为7.32%-21.71%,变异系数为17.46%。11S/7S比值平均值为1.78±0.33,变异幅度为1.46%-3.45%,变异系数为18.55%,差异较大。11S、7S含量与蛋白质和脂肪含量没有相关性。可以看出大豆蛋白亚基相对含量随品种和产地变化存在明显的变异。同时发现4份自然变异的特异大豆种质,为专用型优质大豆品种的选育及大豆食品加工原料的选择提供重要的参考种质。     

Release of glucose-containing polymannose oligosaccharides during glycoprotein biosynthesis. Studies with thyroid microsomal enzymes and slices

Incubations of thyroid microsomes with radiolabeled dolichyl pyrophosphoryl oligosaccharide (Glc3Man9-GlcNAc2) under conditions optimal for the N-glycosylation of protein resulted in the release, by apparently independent enzymatic reactions, of two types of neutral glucosylated polymannose oligosaccharides which differed from each other by terminating either in an N-acetylglucosamine residue (Glc3Man9GlcNAc1) or a di-N-acetylchitobiose moiety (Glc3Man9GlcNAc2). The first mentioned oligosaccharide, which was released in a steady and slow process unaffected by the addition of EDTA, appeared to be primarily the product of endo-beta-N-acetylglucosaminidase action on newly synthesized glycoprotein and such an enzyme with a neutral pH optimum capable of hydrolyzing exogenous glycopeptides and oligosaccharides (Km = 18 microM) was found in the thyroid microsomal fraction. The Glc3Man9GlcNAc2 oligosaccharide, in contrast, appeared to originate from the oligosaccharide-lipid by a rapid hydrolysis reaction which closely paralleled the N-glycosylation step, progressing as long as oligosaccharide transfer to protein occurred and terminating when carbohydrate attachment ceased either due to limitation of lipid-saccharide donor or addition of EDTA. There was a striking similarity between oligosaccharide release and transfer to protein with lipid-linked Glc3Man9GlcNAc2 serving as a 10-fold better substrate for both reactions than lipid-linked Man9-8GlcNAc2. The coincidence of transferase and hydrolase activities suggest the possibility of the existence of one enzyme with both functions. The physiological relevance of oligosaccharide release was indicated by the formation of such molecules in thyroid slices radiolabeled with [2-3H]mannose. Large oligosaccharides predominated (12 nmol/g) and consisted of two families of components; one group terminating in N-acetylglucosamine, ranged from Glc1Man9GlcNAc1 to Man5GlcNAc1 while the other contained the di-N-acetylchitobiose sequence and included Glc3Man9GlcNAc2, Glc1Man9GlcNAc2, and Man9GlcNAc2.     

Carbohydrate structures of HVJ (Sendai virus) glycoproteins

The carbohydrate structures of two membrane glycoproteins (HANA protein and F protein) of HVJ have been determined on materials purified from virions grown in the allantoic sac of embryonated chicken eggs. Both glycoproteins contain fucose, mannose, galactose, and glucosamine but not galactosamine, indicating that their sugar chains are exclusively of the asparagine-linked type. The radioactive oligosaccharide fractions obtained from the two glycoproteins by hydrazinolysis followed by NaB[3H]4 reduction gave quite distinct fractionation patterns after paper electrophoresis. More than 75% of the oligosaccharides from F protein were acidic and separated into at least four components by paper electrophoresis. Only 18% of the oligosaccharide from HANA protein was an acidic single component. These acidic oligosaccharides could not be converted to neutral oligosaccharides by sialidase digestion. Structural studies of the neutral oligosaccharide fractions from HANA and F proteins revealed that both of them are mixtures of a series of high mannose type oligosaccharides and of complex type oligosaccharides with Gal beta 1 leads to (Fuc alpha 1 leads to 3) GlcNAc group in their outer chain moieties.     

Carbohydrate components of lipovitellin of the sand crab Emerita asiatica

Lipovitellin II (Lv II), the major yolk protein of the anomuran crab Emerita asiatica, was purified using heparin-sepharose affinity column chromatography. The purified Lv II was a glycoprotein as it was stainable with periodic acid-Schiff's reagent. Quantitative analysis of sugars showed the presence of fucose, mannose, galactosamine, N-linked oligosaccharides, as well as O-linked oligosaccharides containing N-acetyl hexosamine as the terminal residue. The amount of N-linked oligosaccharides is higher than that of the O-linked oligosaccharides. Biogel P-4 column chromatographic separation of the radiolabeled oligosaccharides of Lv II showed the presence of five different O-linked oligosaccharides and four different N-linked oligosaccharide species. HPTLC separation of the neoglycolipids prepared from the O-linked oligosaccharides also showed the presence of five different O-linked oligosaccharide species. N-linked oligosaccharides contain significant quantities of mannose. Unisil column chromatographic purification in conjunction with HPTLC separation revealed three neutral glycolipid species such as monoglycosylceramide, diglycosylceramide, and triglycosylceramide in the Lv II. The functional significance of these carbohydrate components of the major yolk protein during embryogenesis of the sand crab is discussed.     

Effect of rj1rj1 (non-nodulating) soybeans on nodulation of near isogenic Rj1Rj1 plants in nutrient culture

An earlier proposal (Can. J. Microbiol. 7: 851; 1961) that rj1rj1 (non-nodulating) soybeans (Glycine max (L.) Merr.) excrete a substance that inhibits nodulation of Rj1 Rj1 (nodulating) plants was tested. Using near isogenic lines (isolines) of "Clark" and "Harosoy" soybeans, we consistently found nonsignificant reduction in nodule number and acetylene reduction per Rj1Rj1 plant grown in association with their rj1rj1 counterparts: these results suggest that a nodulation inhibitor is not associated with the rj1 gene. Reducing the number of plants grown in each pot produced significant (P = 0.05) reductions in nodule number per Rj1Rj1 plant, and resembled the observations of the earlier report. On this basis, we suggest that the reported inhibition of nodulation was due to a failure to detoxify or remove an inhibitor (possibly nitrate) already present in the nutrient solution. Both Clark isolines removed nitrate from their nutrient solutions at similar rates. Harosoy rj1rj1 plants removed nitrate at a significantly (P - 0.05) slower rate than Harosoy Rj1Rj1 plants, but the differences were not correlated (P = 0.05) with the small observed decreases in nodulation. These differences in nitrate uptake were highly correlated (P = 0.01) with reduced dry weight per Harosoy rj1rj1 plant.     

Comparison of oligosaccharides derived from salivary mucin of Japanese secretor and non-secretor individuals of blood group type-A

Comparison of oligosaccharide components derived from salivary mucin was performed between secretor and non-secretor individuals. Salivary mucin was collected from four secretors and three non-secretors having blood group type-A. Compositional analysis showed that the contents of galactose and N-acetylglucosamine in the non-secretor were higher than those in the secretor. The O-linked oligosaccharides obtained by treatment with alkaline borohydride were separated by gel filtration using Sephadex G-50. The results indicated that the size of the type-A active oligosaccharides from the secretor was similar to or smaller than that of the non-secretor. Ion-exchange chromatography showed that the secretors had strong type-A activities in both the neutral and acidic fractions but the non-secretors showed type-A activity mainly in the neutral fraction. These results suggest that compositional differences in blood group substances exist between secretors and non-secretors.     

Comparative structural study of the N-linked oligosaccharides of human normal and pathological immunoglobulin G

The structures of oligosaccharides of normal and pathological immunoglobulin G (IgG) are reported. Asparagine-linked neutral oligosaccharides were released by N-oligosaccharide glycopeptidase (almond) digestion. The reducing ends of the oligosaccharide chains thus obtained were aminated with a fluorescent reagent, 2-aminopyridine, and the mixture of pyridylamino derivatives of the oligosaccharides was separated by reverse-phase high-performance liquid chromatography. It was possible to separate 15 out of the 16 kinds of oligosaccharides that have been suggested to exist in normal human IgG. High-resolution proton nuclear magnetic resonance spectroscopy was used along with chemical methods to determine the structures of the separated oligosaccharides. It has been shown that in normal IgG a biantennary complex-type oligosaccharide with a fucose residue (formula; see text) is predominant and four kinds of oligosaccharides, which are biantennary with bisecting N-acetylglucosamine and without fucose residues, exist only in a very small quantity. The results obtained for normal IgG were compared with those obtained for three myeloma IgG proteins. It has been found that the most abundant species that exist in the pathological proteins analyzed in the present work lack one or two galactose residues at the nonreducing terminal. We show that the fractions of fucose-containing oligosaccharides are markedly decreased in the heavy-chain disease protein Per. It is of particular interest that in this paraprotein the major component is a biantennary complex-type oligosaccharide that lacks a fucose residue and an oligosaccharide with the structure (Formula: see text) exists as one of the most abundant components.     

Release of polymannose oligosaccharides from vesicular stomatitis virus G protein during endoplasmic reticulum-associated degradation

To further explore the localization of the N-deglycosylation involved in the endoplasmic reticulum (ER)-associated quality control system we studied HepG2 cells infected with vesicular stomatitis virus (VSV) and its ts045 mutant, as in this system oligosaccharide release can be attributed solely to the VSV glycoprotein (G protein). We utilized the restricted intracellular migration of the mutant protein as well as dithiothreitol (DTT), low temperature, and a castanospermine (CST)-imposed glucosidase blockade to determine in which intracellular compartment deglycosylation takes place. Degradation of the VSV ts045 G protein was considerably greater at the nonpermissive than at the permissive temperature; this was reflected by a substantial increase in polymannose oligosaccharide release. Under both conditions these oligosaccharides were predominantly in the characteristic cytosolic form, which terminates in a single N-acetylglucosamine (OS-GlcNAc(1)); this was also the case in the presence of DTT, which retains the G protein completely in the ER. However when cells infected with the VSV mutant were examined at 15 degrees C or exposed to CST, both of which represent conditions that impair ER-to-cytosol transport, the released oligosaccharides were almost exclusively (> 95%) in the vesicular OS-GlcNAc(2) form; glucosidase blockade had a similar effect on the wild-type virus. Addition of puromycin to glucosidase-inhibited cells resulted in a pronounced reduction (> 90%) in oligosaccharide release, which reflected a comparable impairment in glycoprotein biosynthesis and indicated that the OS-GlcNAc(2) components originated from protein degradation rather than hydrolysis of oligosaccharide lipids. Our findings are consistent with N-deglycosylation of the VSV G protein in the ER and the subsequent transport of the released oligosaccharides to the cytosol where OS-GlcNAc(2) to OS-GlcNAc(1) conversion by an endo-beta-N-acetylglucosaminidase takes place. Studies with the ts045 G protein at the nonpermissive temperature permitted us to determine that it can be processed by Golgi endomannosidase although remaining endo H sensitive, supporting the concept that it recycles between the ER and cis-Golgi compartments.     

Structural characterization of the oligosaccharides of a human monoclonal anti-lipopolysaccharide immunoglobulin M

The oligosaccharide side chains of a human anti-lipopolysaccharide IgM produced by a human-human-mouse heterohybridoma were analyzed at each of its five conserved N-glycosylation sites. This antibody also has a potential sixth N-glycosylation site in the variable region of its heavy chain which is not glycosylated. The oligosaccharides were released by digestion with various endo- and exoglycosidases and analyzed by matrix-assisted laser desorption/ionization-time of flight mass spectrometry and fluorophore-assisted carbohydrate electrophoresis. The antibody has various complex- and hybrid-type oligosaccharide structures at Asn 171, various sialylated complex-type oligosaccharides at Asn 332 and 395, and high-mannose-type oligosaccharides at Asn 402 and 563. Of note is the presence in this human IgM of oligosaccharides containing N-glycolylneuraminic acid and N-acetylneuraminic acid in the ratio of 98:2 as determined using anion- exchange chromatography. Furthermore, we observed oligosaccharide structures containing Gal alpha (1,3)Gal that have not been reported as components of human glycoproteins.      

Oligosaccharides of the Hazelhurst vesicular stomatitis virus glycoprotein are more extensively processed in Rous sarcoma virus-transformed baby hamster kidney cells

Because of the extensive oligosaccharide heterogeneity of the membrane glycoprotein (G) from the Hazelhurst strain of vesicular stomatitis virus, this virus has been used as a specific intracellular probe of altered protein glycosylation in Rous sarcoma virus-transformed versus normal baby hamster kidney cells. Over 70% of G protein from virus released from the transformed cells had acidic-type oligosaccharides at both glycosylation sites, compared to less than 50% from the corresponding normal host cells. The remaining G protein contained an acidic-type oligosaccharide at one site and an endo-beta-N-acetylglucosaminidase H-sensitive oligosaccharide at the other. The major endoglycosidase-sensitive species were sialylated hybrid-type (NeuNAc-Gal-GlcNAc-Man5GlcNAc2-Asn) from the transformed and neutral-type (Man5-6GlcNAc2-Asn) from the normal host cells. The degree of branching of the acidic-type oligosaccharides was not increased in the transformed cells (approx. 80% biantennary for viral G protein from both cell types). At a reduced growth temperature (24 versus 37 degrees C), the G protein oligosaccharides were more extensively processed in both cell types (approximately 85-95% of G protein contained acidic-type structures at both sites), even though the level of viral protein synthesis and virus release was decreased. Essentially all of the minor, endoglycosidase-sensitive oligosaccharides on mature viral G protein were sialic acid-containing hybrid-type structures. At 24 degrees C the branching of the acidic-type oligosaccharides was increased in the virus released from the transformed cells versus normal cells.     

Glycosylation and intracellular transport of membrane glycoproteins encoded by murine leukemia viruses. Inhibition by amino acid analogues and by tunicamycin

Addition of asparagine-linked oligosaccharides to nascent murine leukemia virus (MuLV)-encoded membrane glycoproteins was inhibited either completely by tunicamycin or specifically at Asn-X-Thr glycosylation sites by incorporation of the threonine analogue beta-hydroxynorvaline. In conditions of partial analogue substitution, a series of subglycosylated components is formed which are related by a constant apparent Mr difference when assayed by polyacrylamide gel electrophoresis in the presence of sodium dodecyl sulfate. The total number of asparagine-linked oligosaccharides is then estimated by dividing the measured apparent Mr of one oligosaccharide into the total apparent Mr difference between the complete glycoprotein and the polypeptide chain that is synthesized in cells incubated with tunicamycin. Correct results were obtained using glycoproteins with known numbers of oligosaccharides. Our analyses indicate that the gp70 membrane envelope glycoproteins of certain ecotropic MuLVs contain seven oligosaccharides, whereas the GIX+ antigen-containing variant gp70 contains one fewer Asn-X-Thr-linked oligosaccharide. The membrane glycoprotein encoded by the gag gene of Friend MuLV contains only one asparagine-linked oligosaccharide. Similarly, the gp55 membrane glycoprotein encoded by Friend erythroleukemia virus contains four asparagine-linked oligosaccharides. Pulse-chase and cell surface iodination analyses indicate that MuLV membrane envelope glycoprotein processing by partial proteolysis and transport to the cell surface can be efficiently blocked by structural perturbations caused by incorporation of different amino acid analogues or by loss of oligosaccharides. Our data also suggest that loss of oligosaccharides may expose new antigenic sites in viral membrane glycoproteins and increase their susceptibility to intracellular proteolysis.