不同种属动物肠道糖基化模式及其对大豆凝集素敏感性研究
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摘要
本论文共包括四个部分：研究了不同种属动物猪、鸡、兔等肠道糖基化模式,分离鉴定了肠道大豆凝集素受体,建立高效廉价的大豆凝集素亲和层析体系并纯化大豆凝集素,研究了日粮添加大豆凝集素对不同种属动物肠道糖基化的影响。
本试验利用定量凝集素组织化学技术以生物素标记的大豆凝集素(SBA)、麦胚凝集素(WGA)、刀豆凝集素(ConA)、蓖麻凝集素(RCA)、荆豆凝集素(UEA)为探针对1/4性成熟猪、鸡、兔三种动物的十二指肠、空肠前段、空肠中段、空肠后段、回肠等各段糖基组成进行了刻画,并对各种属动物肠道部位、细胞类型等的糖基化进行了比较。结果：生物素标记的WGA、WGA、ConA、RCA与猪、兔和鸡的肠道组织都有结合,UEA只与外猪、兔肠道组织结合,而未与鸡肠道组织结合。凝集素结合的细胞类型主要为杯状细胞、柱状上皮细胞和少量淋巴细胞,但不同凝集素与同种细胞类型结合存在量的差异；同种动物的不同消化道区段各凝集素在的结合规律也不尽相同；不同种属动物的同一消化道区段也存在差异。结果表明：猪、兔和鸡的肠道各段均存在N-乙酰基葡萄糖胺、N-乙酰基-D-半乳糖胺、半乳糖、甘露糖糖基,而岩藻糖糖基仅存在猪和兔消化道各段,并不存在于鸡消化道各段。N-乙酰基葡萄糖胺、半乳糖、甘露糖糖基、N-乙酰基-D-半乳糖胺糖在猪、兔和鸡不同种属动物肠道的杯状细胞、柱状细胞和少量淋巴细胞均有分布。岩藻糖基除鸡也外分布于上述细胞。在各细胞类型中N-乙酰基-D-半乳糖胺主要分布于肠道上皮的柱状细胞和杯状细胞膜的游离侧面。各种属动物小肠各段优势糖基存在差异：如猪肠道为岩藻糖和甘露糖,鸡肠道为N-乙酰基葡萄糖胺和半乳糖,兔肠道为岩藻糖和N-乙酰基葡萄糖胺。另外肠道各段糖基的组成比例也存在差异。各种属动物糖基化水平也存在差异如鸡肠道除岩藻糖为阴性外,其他糖基化水平相对含量均高于猪、兔肠道各段。
试验选取新生未哺乳的猪和兔及新生未采食的仔鸡,分离肠道上皮组织并提取膜蛋白,采用大豆凝集素亲和层析技术,从上述膜蛋白粗提物中分离能与大豆凝集素特异性结合糖蛋白(大豆凝集素受体),用双向电泳将“糖捕获”法分离获得的大豆凝集素受体蛋白的分子量和等电点等信息并将各组分进一步分离,最后选取代表性的双向电泳斑点进行质谱(MS-TOF/TOF)鉴定。结果：大豆凝集素亲和层析结合双向电泳技术分离获得了猪、鸡、兔的肠道上皮组织蛋白大豆凝集素受体蛋白的表达谱。猪的大豆凝集素受体蛋白多分布于PI5-8,MW30kD-97.2kD区域,切取13蛋白点,经质谱鉴定和IPI数据库搜库分析比对,共获得11个已验证蛋白,分别为内源凝集素1β蛋白、内源凝集-2、Ⅰ和Ⅱ型细胞支架蛋白、膜联蛋白A4、模板激活蛋白、78kD葡萄糖调节蛋白、71kD同源热休克蛋白、钙激活的氯化物通道调节蛋白。鸡的大豆凝集素受体多分布在PI5-8,MW29.0kD-64.2kD区域,切取18蛋白点,经串联质谱鉴定和IPI数据库检索,获得12个已验证蛋白,有9个具有催化功能的酶蛋白：L-乳酸脱氢酶、蛋白质二硫化异构酶A3、磷酸丙糖异构酶、叶酸合成蛋白、视黄醛脱氢酶1、U型肌酸激酶、ATP合成酶p亚基、苹果酸脱氢酶、膜联蛋白2,1个与细胞结构功能相关的蛋白,细胞骨架蛋白,1个热休克蛋白。兔的大豆凝集素受体蛋白多分布于PI5-8,MW26.0kD-90.0kD区域,质潜鉴定和IPI数据库检索分析,获得3个蛋白,分别为解螺旋蛋白、肌动蛋白、Ⅰ型细胞骨架蛋白。
为获取大量纯化的大豆凝集素已满足动物实验需要,本试验以D-半乳糖胺为配基,以FF-sepharose4B为固定相,制备大豆凝集素亲和层析填料。建立了高效廉价的大豆凝集素纯化体系,测定了所纯化大豆凝集素的纯度、免疫原性和凝集活性,并与Sigma标准品进行了比较。结果：所用纯化体系具有高纯化效率,每毫升GalN-FF-sepharose-4B层析填料能结合10mg大豆凝集素；所得的大豆凝集素亚基的分子量为30kD, SDS-PAGE测定纯度在98%以上,Western blot结果为阳性,1mg/mL SBA血集效价为1/210,各指标与理论值相符,且与Sigma大豆凝集素标准品一致。
本实验选限1/4性成熟猪、鸡、兔,各分成5组,分别饲喂含大豆凝集素质量浓度为0,0.025%,0.25%,0.5%和1%的纯合日粮,饲喂结束后,以生物素标记的大豆凝集素为探针检测了上述三种动物不同肠段的N-乙酰基D-半乳糖胺的变化情况。结果：日粮中添加大豆凝集素能够引起动物肠道内N-乙酰基D-半乳糖胺的变化,三种动物肠道的N-乙酰基D-半乳糖胺随日粮大豆凝集素的浓度升高表达量增加,1%大豆凝集素添加组不同种属动物肠道各段N-乙酰基D-半乳糖胺表达量显著高于对照组(P<0.05)。猪肠道N-乙酰基D-半乳糖胺含量从十二指肠到回肠呈现降低趋势,十二指肠和空肠前段N-乙酰基D-半乳糖胺对大豆凝集素敏感性较空肠中、后段和回肠强。鸡肠道N-乙酰基D-半乳糖胺含量从十二指肠到回肠呈现上升趋势,同一肠段随着大豆凝集素刺激剂量的升高糖基化水平也呈逐渐升高的趋势,空肠前段和中段敏感性较其他肠段强。兔肠道各段随大豆凝集素剂量的增加N-乙酰基D-半乳糖胺含量呈现上升趋势,空肠前段和中段对高浓度大豆凝集素的刺激糖基变化较敏感。
本论文研究表明,不同种属动物肠道糖基类型、糖基含量、优势糖基均存在种属差异。研究发现所选哺乳类代表动物猪和兔的肠道中含有测试的5种糖基,禽类代表动物鸡肠道中含有4种糖基,不含有岩藻糖糖基。三种动物肠道大豆凝集素结合的N-乙酰基-D-半乳糖胺主要结合于肠上皮的柱状细胞和杯状细胞膜的游离侧面。根据三种动物肠道糖基化模式可知,N-乙酰基-D-半乳糖胺不是三种动物肠道的优势糖基。根据鉴定的不同种属肠道上皮结合的大豆凝集素受体蛋白的结构和功能信息,可将其分为三类,一类是细胞膜结构蛋白,一类为功能性调节蛋白,另一类为具有催化活性的酶蛋白。预示大豆凝集素的抗营养作用可能与其结合的蛋白功能有关。大豆凝集素刺激下不同种属动物肠道N-乙酰基D-半乳糖胺的糖基化水平均显著提高,说明大豆凝集素能够对不同种属动物肠道N-乙酰基D-半乳糖胺糖基化水平起到上调作用,肠道N-乙酰基D-半乳糖胺糖基化水平与大豆凝集素的抗营养作用相关,且不同种属动物肠道各段N-乙酰基D-半乳糖胺对大豆凝集素敏感性存在差异。
This research is composed of4parts, the depiction of intestinal glycosylation patterns in different animal species, isolation and identification of SBA receptors, establishment of a kind of affinity chromatography method with high efficiency for SBA purification and detection of the effects of SBA on the intestinal glycosylation of different animal species.
In this research, biotin labeled SBA, WGA, Con A, RCA, and UEA were used as probes in Lectin-histochemical staining to depict the glycosylation patterns in duodenum, pre-jejunum, mid-jejunum, post-jejunum, ileum in pig, chicken and rabbit at1/4sexual maturity stage. The comparison of glycosylation patterns was performed between different intestinal tracts and cell types. Results:biotin labeled SBA, WGA, ConA, RCA and UEA can bind to all tracts of intestine in pig and rabbit. In chicken, all biotin labeled lectins except UEA can bind to all tracts of intestine. The main cell types that lectins can bind to are goblet cells, Columnar epithelial cells and some lymphocytes. Meanwhile, significant differences can be found between the positive signals of different lectins in one cell type. Our results also show that had differences in the quality of positive signals of one lectin between different intestinal tracts in one kind of animal and between the same intestinal tracts in different kinds of animals. It showed that in all intestinal tracts in pigs, rabbits and chickens, N-acetyl-D-glucosamine, N-acetyl-D-galactosamine, galactose, mannose can be detected, and fucose can be found in pigs and rabbits but not in chickens. N-acetyl-D-galactosamine residues that can be recognized by SBA are distributed in the free surface of goblet cells and columnar epithelial cells. Differences can be found between the main glycol-residues in different kinds of animals, in pig intestine, the main residues are fucoses and mannoses, in rabbits, are fucose and N-acetyl-D-glucosamine. and in chicken are N-acetyl-D-glucosamine and galactose, respectively. In chikens, there are more N-acetyl-D-glucosamine, N-Acetyl-D-galactosamine, galactose, mannose than other two kinds of animals.
Then new born and not breast-feeding pigs, rabbits and chickens were chosen in this research, and crude membrane proteins were isolated from intestinal tissue and then SBA receptors in the intestine in these animals were purified by SBA affinity chromatography;2-D electrophoresis was performed and MW and pI of SBA receptors that purified by glycol-capture method were obtained. At last, glycoproteins were identified through MS-TOF/TOF. Results:the expression map of SBA receptors was obtained by the means of SBA affinity chromatography and2-D electrophoresis. pI of SBA receptors in piglets are distributed in the range of5-8, and MV30kD-97.2kD. Among those glycoproteins13proteins were chosen for MS-TOF/TOF, after identification and blast in IPI base,11known protein were identified, which were named as Intelectin-1β,Keratin, pattern Ⅱ cytoskeletal1, Keratin, pattern Ⅰ cytoskeletal10,Annexin A4, Protein SET,78kD glucose-regulated protein, Heat shock cognate71kD protein, Calcium-activated chloride channel regulator1. pI of SBA receptors in chickens is located in the range of5-8, and MW29.0kD-64.2kD. Among those proteins18dots were cut, after MS-TOF/TOF identification and blast in IPI base,12known proteins were identified, and among which9proteins were enzyme proteins with catalytic activity such as L-lactate dehydrogenase A chain. Protein disulfide-isomerase A3, Triosephosphate isomerase, Folic acid synthesis protein FOL1, Creatine kinase U-pattern, mitochondrial, ATP synthase subunit β,mitochondrial, Malate dehydrogenase, Annexin A2. A cell structure and function of protein, Keratin, pattern Ⅱ cytoskeletal1, and one HSP. PI of SBA receptors in rabbits intestine was located in the range of5-8, and MV in the range of26.0kD-90.0kD, after MS-TOF/TOF and blast in IPI base,3protein were identified with the names of helix-destabilizing protein,actin, type Ⅰ cytoskeletal9.
In order to obtain enough SBA for animal experiment, D-galactose-FF-sepharose4B was synthesized as an affinity adsorbent for affinity chromatography. SBA was purified in this system, and the purity, immunogenicity, hemagglutinational activity were detected and compared with standard SBA. Results:the affinity activity of GalN-FF-sepharose-4B is lOmgSBA per ml. The MV of the SBA we purified is30kD, purity is98%. Western blot shows the purified SBA is active. hemagglutinational activity value is1/210. There are no difference of the purity, immunogenicity and hemagglutinational activity between theSBA that we obtained and the standard SBA.
In this research,1/4sexual maturity piglets, chickens and rabbits were, and divided into five groups and then were feed with diet containing SBA with the concentration of0,0.025%,0.25%,0.50%and1.00%respectively. Lectin-histochemical staining was performed as described in experiment Ⅰ. the change of N-acetyl-D-glucosamine was detected through the biotin labeled SBA as probe. Results:N-acetyl-D-glucosamine in the intestine can be changed by feed diet containing SBA. N-acetyl-D-glucosamine in all the animals intestine can be increased by SBA, and in1%group, all intestinal tracts in all kind of animals, the expression of N-acetyl-D-glucosamine glycosylation is significantly higher than that of control group(P<0.05). The trend of N-Acetyl-D-galactosamine in piglet intestine is decreased from duodenum to ileum, and the sensitivities in duodenum and pre-jejunum, were higher than that of mid-jejunum, post-jejunum and ileum. In the intestine of chickens, the trend of N-Acetyl-D-galactosamine was increased from duodenum to ileum, and the sensitivities of pre-jejunum and mid-jejunum were higher than other tracts. In rabbits, N-Acetyl-D-galactosamine was increased by the raise SBA contention.
This study showed that there are many differences in the glycol-patterns, quantity of glycol-residues, and dominant glycol-residues between different animal species. It showed that in intestine in piglets and rabbits which stand for mammalian, all5kinds of glycol-residues can be detected and in chickens which stand for poultry only4kinds of glycol-residues can be detected. The distribution of glycol-residues is located in the free surface of goblet cells, Columnar epithelial cells in all animals that were used in this study According to intestinal glycol-pattern in these three kinds of animals, N-Acetyl-D-galactosamine residues are not the dominant glycol-residues. According to the structural and functional information, the proteins can be divided into3classes, cell membrane structural proteins, functional regulating proteins, and enzyme proteins with catalytic activities. These results elucidated that the anti-nutrition activities of SBA may be mediated by their binding proteins. The increase of N-Acetyl-D-galactosamine in intestine of different animals illustrate that SBA can regulate the level of the expression of N-Acetyl-D-galactosamine, that may associated with the anti-nutrition of SBA, and the sensitivity to SBA is dependent on the kind of animals and the tracts of the intestine.
本试验利用定量凝集素组织化学技术以生物素标记的大豆凝集素(SBA)、麦胚凝集素(WGA)、刀豆凝集素(ConA)、蓖麻凝集素(RCA)、荆豆凝集素(UEA)为探针对1/4性成熟猪、鸡、兔三种动物的十二指肠、空肠前段、空肠中段、空肠后段、回肠等各段糖基组成进行了刻画,并对各种属动物肠道部位、细胞类型等的糖基化进行了比较。结果：生物素标记的WGA、WGA、ConA、RCA与猪、兔和鸡的肠道组织都有结合,UEA只与外猪、兔肠道组织结合,而未与鸡肠道组织结合。凝集素结合的细胞类型主要为杯状细胞、柱状上皮细胞和少量淋巴细胞,但不同凝集素与同种细胞类型结合存在量的差异；同种动物的不同消化道区段各凝集素在的结合规律也不尽相同；不同种属动物的同一消化道区段也存在差异。结果表明：猪、兔和鸡的肠道各段均存在N-乙酰基葡萄糖胺、N-乙酰基-D-半乳糖胺、半乳糖、甘露糖糖基,而岩藻糖糖基仅存在猪和兔消化道各段,并不存在于鸡消化道各段。N-乙酰基葡萄糖胺、半乳糖、甘露糖糖基、N-乙酰基-D-半乳糖胺糖在猪、兔和鸡不同种属动物肠道的杯状细胞、柱状细胞和少量淋巴细胞均有分布。岩藻糖基除鸡也外分布于上述细胞。在各细胞类型中N-乙酰基-D-半乳糖胺主要分布于肠道上皮的柱状细胞和杯状细胞膜的游离侧面。各种属动物小肠各段优势糖基存在差异：如猪肠道为岩藻糖和甘露糖,鸡肠道为N-乙酰基葡萄糖胺和半乳糖,兔肠道为岩藻糖和N-乙酰基葡萄糖胺。另外肠道各段糖基的组成比例也存在差异。各种属动物糖基化水平也存在差异如鸡肠道除岩藻糖为阴性外,其他糖基化水平相对含量均高于猪、兔肠道各段。
试验选取新生未哺乳的猪和兔及新生未采食的仔鸡,分离肠道上皮组织并提取膜蛋白,采用大豆凝集素亲和层析技术,从上述膜蛋白粗提物中分离能与大豆凝集素特异性结合糖蛋白(大豆凝集素受体),用双向电泳将“糖捕获”法分离获得的大豆凝集素受体蛋白的分子量和等电点等信息并将各组分进一步分离,最后选取代表性的双向电泳斑点进行质谱(MS-TOF/TOF)鉴定。结果：大豆凝集素亲和层析结合双向电泳技术分离获得了猪、鸡、兔的肠道上皮组织蛋白大豆凝集素受体蛋白的表达谱。猪的大豆凝集素受体蛋白多分布于PI5-8,MW30kD-97.2kD区域,切取13蛋白点,经质谱鉴定和IPI数据库搜库分析比对,共获得11个已验证蛋白,分别为内源凝集素1β蛋白、内源凝集-2、Ⅰ和Ⅱ型细胞支架蛋白、膜联蛋白A4、模板激活蛋白、78kD葡萄糖调节蛋白、71kD同源热休克蛋白、钙激活的氯化物通道调节蛋白。鸡的大豆凝集素受体多分布在PI5-8,MW29.0kD-64.2kD区域,切取18蛋白点,经串联质谱鉴定和IPI数据库检索,获得12个已验证蛋白,有9个具有催化功能的酶蛋白：L-乳酸脱氢酶、蛋白质二硫化异构酶A3、磷酸丙糖异构酶、叶酸合成蛋白、视黄醛脱氢酶1、U型肌酸激酶、ATP合成酶p亚基、苹果酸脱氢酶、膜联蛋白2,1个与细胞结构功能相关的蛋白,细胞骨架蛋白,1个热休克蛋白。兔的大豆凝集素受体蛋白多分布于PI5-8,MW26.0kD-90.0kD区域,质潜鉴定和IPI数据库检索分析,获得3个蛋白,分别为解螺旋蛋白、肌动蛋白、Ⅰ型细胞骨架蛋白。
为获取大量纯化的大豆凝集素已满足动物实验需要,本试验以D-半乳糖胺为配基,以FF-sepharose4B为固定相,制备大豆凝集素亲和层析填料。建立了高效廉价的大豆凝集素纯化体系,测定了所纯化大豆凝集素的纯度、免疫原性和凝集活性,并与Sigma标准品进行了比较。结果：所用纯化体系具有高纯化效率,每毫升GalN-FF-sepharose-4B层析填料能结合10mg大豆凝集素；所得的大豆凝集素亚基的分子量为30kD, SDS-PAGE测定纯度在98%以上,Western blot结果为阳性,1mg/mL SBA血集效价为1/210,各指标与理论值相符,且与Sigma大豆凝集素标准品一致。
本实验选限1/4性成熟猪、鸡、兔,各分成5组,分别饲喂含大豆凝集素质量浓度为0,0.025%,0.25%,0.5%和1%的纯合日粮,饲喂结束后,以生物素标记的大豆凝集素为探针检测了上述三种动物不同肠段的N-乙酰基D-半乳糖胺的变化情况。结果：日粮中添加大豆凝集素能够引起动物肠道内N-乙酰基D-半乳糖胺的变化,三种动物肠道的N-乙酰基D-半乳糖胺随日粮大豆凝集素的浓度升高表达量增加,1%大豆凝集素添加组不同种属动物肠道各段N-乙酰基D-半乳糖胺表达量显著高于对照组(P<0.05)。猪肠道N-乙酰基D-半乳糖胺含量从十二指肠到回肠呈现降低趋势,十二指肠和空肠前段N-乙酰基D-半乳糖胺对大豆凝集素敏感性较空肠中、后段和回肠强。鸡肠道N-乙酰基D-半乳糖胺含量从十二指肠到回肠呈现上升趋势,同一肠段随着大豆凝集素刺激剂量的升高糖基化水平也呈逐渐升高的趋势,空肠前段和中段敏感性较其他肠段强。兔肠道各段随大豆凝集素剂量的增加N-乙酰基D-半乳糖胺含量呈现上升趋势,空肠前段和中段对高浓度大豆凝集素的刺激糖基变化较敏感。
本论文研究表明,不同种属动物肠道糖基类型、糖基含量、优势糖基均存在种属差异。研究发现所选哺乳类代表动物猪和兔的肠道中含有测试的5种糖基,禽类代表动物鸡肠道中含有4种糖基,不含有岩藻糖糖基。三种动物肠道大豆凝集素结合的N-乙酰基-D-半乳糖胺主要结合于肠上皮的柱状细胞和杯状细胞膜的游离侧面。根据三种动物肠道糖基化模式可知,N-乙酰基-D-半乳糖胺不是三种动物肠道的优势糖基。根据鉴定的不同种属肠道上皮结合的大豆凝集素受体蛋白的结构和功能信息,可将其分为三类,一类是细胞膜结构蛋白,一类为功能性调节蛋白,另一类为具有催化活性的酶蛋白。预示大豆凝集素的抗营养作用可能与其结合的蛋白功能有关。大豆凝集素刺激下不同种属动物肠道N-乙酰基D-半乳糖胺的糖基化水平均显著提高,说明大豆凝集素能够对不同种属动物肠道N-乙酰基D-半乳糖胺糖基化水平起到上调作用,肠道N-乙酰基D-半乳糖胺糖基化水平与大豆凝集素的抗营养作用相关,且不同种属动物肠道各段N-乙酰基D-半乳糖胺对大豆凝集素敏感性存在差异。
This research is composed of4parts, the depiction of intestinal glycosylation patterns in different animal species, isolation and identification of SBA receptors, establishment of a kind of affinity chromatography method with high efficiency for SBA purification and detection of the effects of SBA on the intestinal glycosylation of different animal species.
In this research, biotin labeled SBA, WGA, Con A, RCA, and UEA were used as probes in Lectin-histochemical staining to depict the glycosylation patterns in duodenum, pre-jejunum, mid-jejunum, post-jejunum, ileum in pig, chicken and rabbit at1/4sexual maturity stage. The comparison of glycosylation patterns was performed between different intestinal tracts and cell types. Results:biotin labeled SBA, WGA, ConA, RCA and UEA can bind to all tracts of intestine in pig and rabbit. In chicken, all biotin labeled lectins except UEA can bind to all tracts of intestine. The main cell types that lectins can bind to are goblet cells, Columnar epithelial cells and some lymphocytes. Meanwhile, significant differences can be found between the positive signals of different lectins in one cell type. Our results also show that had differences in the quality of positive signals of one lectin between different intestinal tracts in one kind of animal and between the same intestinal tracts in different kinds of animals. It showed that in all intestinal tracts in pigs, rabbits and chickens, N-acetyl-D-glucosamine, N-acetyl-D-galactosamine, galactose, mannose can be detected, and fucose can be found in pigs and rabbits but not in chickens. N-acetyl-D-galactosamine residues that can be recognized by SBA are distributed in the free surface of goblet cells and columnar epithelial cells. Differences can be found between the main glycol-residues in different kinds of animals, in pig intestine, the main residues are fucoses and mannoses, in rabbits, are fucose and N-acetyl-D-glucosamine. and in chicken are N-acetyl-D-glucosamine and galactose, respectively. In chikens, there are more N-acetyl-D-glucosamine, N-Acetyl-D-galactosamine, galactose, mannose than other two kinds of animals.
Then new born and not breast-feeding pigs, rabbits and chickens were chosen in this research, and crude membrane proteins were isolated from intestinal tissue and then SBA receptors in the intestine in these animals were purified by SBA affinity chromatography;2-D electrophoresis was performed and MW and pI of SBA receptors that purified by glycol-capture method were obtained. At last, glycoproteins were identified through MS-TOF/TOF. Results:the expression map of SBA receptors was obtained by the means of SBA affinity chromatography and2-D electrophoresis. pI of SBA receptors in piglets are distributed in the range of5-8, and MV30kD-97.2kD. Among those glycoproteins13proteins were chosen for MS-TOF/TOF, after identification and blast in IPI base,11known protein were identified, which were named as Intelectin-1β,Keratin, pattern Ⅱ cytoskeletal1, Keratin, pattern Ⅰ cytoskeletal10,Annexin A4, Protein SET,78kD glucose-regulated protein, Heat shock cognate71kD protein, Calcium-activated chloride channel regulator1. pI of SBA receptors in chickens is located in the range of5-8, and MW29.0kD-64.2kD. Among those proteins18dots were cut, after MS-TOF/TOF identification and blast in IPI base,12known proteins were identified, and among which9proteins were enzyme proteins with catalytic activity such as L-lactate dehydrogenase A chain. Protein disulfide-isomerase A3, Triosephosphate isomerase, Folic acid synthesis protein FOL1, Creatine kinase U-pattern, mitochondrial, ATP synthase subunit β,mitochondrial, Malate dehydrogenase, Annexin A2. A cell structure and function of protein, Keratin, pattern Ⅱ cytoskeletal1, and one HSP. PI of SBA receptors in rabbits intestine was located in the range of5-8, and MV in the range of26.0kD-90.0kD, after MS-TOF/TOF and blast in IPI base,3protein were identified with the names of helix-destabilizing protein,actin, type Ⅰ cytoskeletal9.
In order to obtain enough SBA for animal experiment, D-galactose-FF-sepharose4B was synthesized as an affinity adsorbent for affinity chromatography. SBA was purified in this system, and the purity, immunogenicity, hemagglutinational activity were detected and compared with standard SBA. Results:the affinity activity of GalN-FF-sepharose-4B is lOmgSBA per ml. The MV of the SBA we purified is30kD, purity is98%. Western blot shows the purified SBA is active. hemagglutinational activity value is1/210. There are no difference of the purity, immunogenicity and hemagglutinational activity between theSBA that we obtained and the standard SBA.
In this research,1/4sexual maturity piglets, chickens and rabbits were, and divided into five groups and then were feed with diet containing SBA with the concentration of0,0.025%,0.25%,0.50%and1.00%respectively. Lectin-histochemical staining was performed as described in experiment Ⅰ. the change of N-acetyl-D-glucosamine was detected through the biotin labeled SBA as probe. Results:N-acetyl-D-glucosamine in the intestine can be changed by feed diet containing SBA. N-acetyl-D-glucosamine in all the animals intestine can be increased by SBA, and in1%group, all intestinal tracts in all kind of animals, the expression of N-acetyl-D-glucosamine glycosylation is significantly higher than that of control group(P<0.05). The trend of N-Acetyl-D-galactosamine in piglet intestine is decreased from duodenum to ileum, and the sensitivities in duodenum and pre-jejunum, were higher than that of mid-jejunum, post-jejunum and ileum. In the intestine of chickens, the trend of N-Acetyl-D-galactosamine was increased from duodenum to ileum, and the sensitivities of pre-jejunum and mid-jejunum were higher than other tracts. In rabbits, N-Acetyl-D-galactosamine was increased by the raise SBA contention.
This study showed that there are many differences in the glycol-patterns, quantity of glycol-residues, and dominant glycol-residues between different animal species. It showed that in intestine in piglets and rabbits which stand for mammalian, all5kinds of glycol-residues can be detected and in chickens which stand for poultry only4kinds of glycol-residues can be detected. The distribution of glycol-residues is located in the free surface of goblet cells, Columnar epithelial cells in all animals that were used in this study According to intestinal glycol-pattern in these three kinds of animals, N-Acetyl-D-galactosamine residues are not the dominant glycol-residues. According to the structural and functional information, the proteins can be divided into3classes, cell membrane structural proteins, functional regulating proteins, and enzyme proteins with catalytic activities. These results elucidated that the anti-nutrition activities of SBA may be mediated by their binding proteins. The increase of N-Acetyl-D-galactosamine in intestine of different animals illustrate that SBA can regulate the level of the expression of N-Acetyl-D-galactosamine, that may associated with the anti-nutrition of SBA, and the sensitivity to SBA is dependent on the kind of animals and the tracts of the intestine.
引文
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