993 resultados para RADIUM 226


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An antimicrobial peptide named odorranain-HP was identified from skin secretions of the diskless odorous frog, Odorrana grahami. It is composed of 23 amino acids with an amino acid sequence of GLLRASSVWGRKYYVDLAGCAKA. By BLAST search, odorranain-HP had si

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本发明涉及一种姚虻唾液腺免疫调节肽及其基因和应用,属于生物医学领域。该免疫调节肽是中国虻科昆虫唾液腺免疫调节肽基因编码的一种线状多肽,其全序列为:甘氨酸-甘氨酸-缬氨酸-丝氨酸-甘氨酸-缬氨酸-丝氨酸-天冬氨酸-苯丙氨酸-谷氨酸-脯氨酸-异亮氨酸-谷氨酸-缬氨酸-丝氨酸- 甘氨酸-谷氨酸-天冬氨酸-酪氨酸-天冬酰胺-丝氨酸-天冬氨酸-谷氨酸 -丙氨酸-天冬氨酸-谷氨酸-天冬氨酸-甘氨酸-赖氨酸-丙氨酸。免疫调节肽基因由362个核苷酸组成,其中编码成熟编码姚虻唾液腺免疫调节肽为第 115-204位核苷酸。该姚虻唾液腺免疫调节肽作为抑制多种细胞因子的应用。本发明的免疫调节肽具有结构简单、人工合成方便、抗菌活性强等特点。

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Thirteen complete and three partial cDNA sequences were cloned from the constructed king cobra (Ophiophagus hannah) venom gland cDNA library. Phylogenetic analysis of nucleotide sequences of king cobra with those from other snake venoms revealed that obta

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Many neuroendocrine peptides that are distributed in amphibian gastrointestinal tract and central nervous system are also found in amphibian skins, and these peptides are classified into skin-gut-brain triangle peptides, such as bombesins, gastrin-releasi

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本发明属于生物医学领域。大蹼铃蟾皮肤肽,是从中国两栖类动物大蹼铃蟾皮肤分泌物中分离得到的一种单链多肽,分子量2674.2,等电点9.8,多肽全序列一级结构为:NH2—GIGTKILGGVKTALKGALKELASTYAN-NH2。其制备方法是将活体大蹼铃蟾用水清洗干净,置于带盖的玻璃容器中,滴加无水乙醚,密闭容器3—5分钟,可见大量的泡沫状物质从大蹼铃蟾皮肤分泌出来,收集分泌物,离心去除沉淀、冷冻干燥后,经离子交换、凝胶过滤柱层析分离纯化后得到。大蹼铃蟾皮肤肽作为制备治微生物感染疾病药物、肿瘤治疗药物的应用。具有显著的抑制细菌和真菌生长、肿瘤细胞抑制活性高等优点。

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Amphibian skin is a rich resource of bioactive peptides like proline-rich bombesin from frog Bombina maxima. A novel cDNA clone encoding a precursor protein that comprises proline-rich bombesin and a novel peptide, designated as bombestatin, was isolated from a skin cDNA library of B. maxima. The predicted primary structure of the novel peptide is WEVLLNVALIRLELLSCRSSKDQDQKESCGMHSW, in which two cysteines form a disulfide bond. A BLAST search of databases did not detect sequences with significant similarity. Bombestatin possesses dose-dependent contractile activity on rat stomach strips. The differences between cDNAs encoding PR-bombesin plus bombestatin and PR-bombesin alone are due to fragment insertions located in 3'-coding region and 3'-untranslational region, respectively. (c) 2005 Elsevier B.V. All rights reserved.

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Despite the evolutional distance between wasp and amphibian, vespid chemotactic peptide (VCP), an important component of wasp venom, are found sharing remarkable similarities with the temporin antimicrobial peptides (AMPs) from Ranid frog, Amolops loloens

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本发明属于生物医学领域。大蹼铃蟾蛋白酶抑制剂,从两栖类动物大蹼铃蟾皮肤中分离得到的一种单链丝氨酸蛋白酶抑制剂,其在SDS-聚丙烯酰胺凝胶电泳上的表观分子量还原条件下为67KDa,非还原条件下为45KDa,等电点4.8,糖含量17—19%,无酶活性,大蹼铃蟾蛋白酶抑制剂的N—端31个氨基酸序列结构是:DSETHIRFLGEVYKKVDTIDFRGLVLITRAQ。其制备方法是取大蹼铃蟾皮肤,在生理盐水中匀浆后,离心去除沉淀,收集上清液冷冻干燥后,经离子交换,凝胶过滤纯化后得到。具有强烈的丝氨酸蛋白酶抑制活性和抗肿瘤活性,作为制备肿瘤治疗药物和制备治疗胃炎、胰腺炎及其他炎症药物的应用。

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A novel protein, named BAS-AH, was purified and characterized from the skin of the toad Bufo andrewsi. BAS-AH is a single chain protein and the apparent molecular weight is about 63 kDa as judged by SDS-PAGE. BAS-AH was determined to bind heme (0.89 mol heme/mol protein) as determined by pyridine haemochrome analysis. Fifty percentage cytotoxic concentration (CC50) of BAS-AH on C8166 cells was 9.5 mu M. However, at concentrations that showed little effect oil cell viability, BAS-AH displayed dose dependent inhibition oil HIV-1 infection and replication. The antiviral selectivity indexes corresponding to the measurements of syncytium formation and HIV-1 p24 (CC50/EC50) were 14.4 and 11.4, respectively, corresponding to the . BAS-AH also showed an inhibitory effect on the activity of recombinant HIV-1 reverse transcriptase (IC50 = 1.32 mu M). The N-terminal sequence of BAS-AH was determined to be NAKXKADVIGKISILLGQDNLSNIVAM, which exhibited little identity with other known anti-HIV-1 proteins. BAS-AH is devoid of antibacterial, protcolytic, trypsin inhibitory activity, (L)-amino acid oxidase activity and catalase activity. (c) 2005 Elsevier Ltd. All rights reserved.

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The disulfide-bridged hendecapeptide ( CWTKSIPPKPC) loop, derived from an amphibian skin peptide, is found to have strong trypsin inhibitory capability. This loop, called the trypsin inhibitory loop ( TIL), appears to be the smallest serine protease inhib

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大蹼铃蟾抗精子多肽及其制备方法和在制药中的应用,属生物医学领域。大蹼铃蟾抗精子多肽,其在聚丙烯酰胺凝胶多肽电泳上的表观分子量还原和非还原条件下为8000Da,等电点8.8;其N-端20个氨基酸残基序列是:AVITGVICRRAQCGVGCAER。制备方法是将活体大蹼铃蟾清洗干净,经收集皮肤分泌物、离心去除沉淀、冷冻干燥、离子交换、凝胶过滤纯化等工序后得到。大蹼铃蟾抗精子多肽具有较强的精子制动活性和丝氨酸蛋白酶抑制活性,作为制备避孕药物和制备治疗胰腺炎及其他炎症药物的应用。

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Amphibian skin secretions contain many bioactive compounds. In the present work, an irreversible serine protease inhibitor, termed baserpin, was purified for the first time from the skin secretions of toad Bufo andrewsi by Successive ion-exchange and gelfiltration chromatography. Baserpin is a single chain glycoprotein, with an apparent molecular weight of about 60 kDa in SDS-PAGE. Baserpin is an irreversible inhibitor and effectively inhibits the catalytic activity of trypsin, chymotrypsin and elastase. SDS-stable baserpin-trypsin complex could be seen in SDS-PAGE indicates that it possibly belongs to the serpin superfamily. According to the association rates determined, baserpin is a potent inhibitor of bovine trypsin (4.6 X 10(6) M-1 S-1), bovine chymotrypsin (8.9 X 10(6) M-1 s(-1)) and porcine elastase (6.8 X 10(6) M-1 s(-1)), whereas it shows no inhibitory effect on thrombin. The N-terminal sequence of baserpin is HTQYPDILIAKPXDK, which shows no similarity with other known serine protease inhibitors. (c) 2005 Elsevier Ltd. All rights reserved.

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Group IIA secretory phospholipases A(2) (sPLA(2)-II) is generally known to display potent grampositive bactericidal activity, while group IA sPLA(2) (sPLA(2)-I) reportedly is not. In this work, a novel sPLA(2)-I named BFPA was identified from Bungarus fas

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本发明涉及大蹼铃蟾抗肿瘤蛋白及其制备方法和其基因,属于生物医学领域。抗肿瘤蛋白是从中国两栖类动物大蹼铃蟾皮肤分泌物中分离得到的一种单链多肽,分子量2697,等电点9.83,多肽氨基酸全序列一级结构为:NH2-GIGGKILSGLKTALKGAAKELASTYLH-NH2。制备方法是收集大蹼铃蟾皮肤分泌物,离心去除沉淀、冷冻干燥后,经离子交换、高压液相反相柱层析分离纯化后得到。由650、623、625个核苷酸组成的三个不同的基因可编码大蹼铃蟾抗肿瘤蛋白,编码成熟抗肿瘤蛋白分别为第177-257位、第166-246位、175-255位核苷酸。具有抑制肿瘤细胞生长、抗艾滋病病毒活性和抑制细菌和真菌生长的作用。

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A novel potent trypsin inhibitor was purified and characterized from frog Bombina maxima skin. A full-length cDNA encoding the protein was obtained from a cDNA library constructed from the skin. Sequence analysis established that the protein actually comprises three conserved albumin domains. B. maxima serum albumin was subsequently purified, and its coding cDNA was further obtained by PCR-based cloning from the frog liver. Only two amino acid variations were found in the albumin sequences from the skin and the serum. However, the skin protein is distinct from the serum protein by binding of a haem b (0.95 mol/mol protein). Different from bovine serum albumin, B. maxima albumin potently inhibited trypsin. It bound tightly with trypsin in a 1: 1 molar ratio. The equilibrium dissociation constants (K-D) obtained for the skin and the serum proteins were 1.92 x 10(-9) M and 1.55 x 10(-9) M, respectively. B. maxima albumin formed a noncovalent complex with trypsin through an exposed loop formed by a disulfide bond (Cys(53)-Cys(62)), which comprises the scissile bond Arg(58)(P-1)-His(59)(P-1'). No inhibitory effects on thrombin, chymotrypsin, elastase, and subtilisin were observed under the assay conditions. Immunohistochemical study showed that B. maxima albumin is widely distributed around the membranes of epithelial layer cells and within the stratum spongiosum of dermis in the skin, suggesting that it plays important roles in skin physiological functions, such as water economy, metabolite exchange, and osmoregulation.