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1.
In this study, several methods were compared for the efficiency to concentrate venom from the tentacles of jellyfish Rhopilema esculentum Kishinouye. The results show that the methods using either freezing-dry or gel absorption to remove water to concentrate
venom are not applicable due to the low concentration of the compounds dissolved. Although the recovery efficiency and the
total venom obtained using the dialysis dehydration method are high, some proteins can be lost during the concentrating process.
Comparing to the lyophilization method, ultrafiltration is a simple way to concentrate the compounds at high percentage but
the hemolytic activities of the proteins obtained by ultrafiltration appear to be lower. Our results suggest that overall
lyophilization is the best and recommended method to concentrate venom from the tentacles of jellyfish. It shows not only
the high recovery efficiency for the venoms but high hemolytic activities as well.
Supported by the Award Foundation of Scientific Research for Excellent Young and Middle-age Scientist of Shandong Province
(No. 2006BS07003) and the Knowledge Innovation Project of Chinese Academy of Sciences (KZCX2-YW-R-104) 相似文献
2.
The present work is the first report of the biochemical characterization of the venom from nematocysts of the jellyfish Rhopilema esculentum Kishinouye. The nematocysts were isolated by autolysis and centrifugation and separated by flow cytometry. Four types of
nematocysts were identified: mastigophores, euryteles, and atrichous and holotrichous isorhiza. SDS-PAGE and amino acid analyses
demonstrated that most of the proteins in the nematocyst extract were between 10 kDa and 40 kDa, and that glutamic acid was
the main amino acid. A hemolytic activity assay showed that the activity of the nematocyst venom (RNV) was strongest in Tris-HCl
buffer (50 mmol/L, pH 7.8, 5% glycerol, 0.5 mmol/L EDTA, 0.1 mol/L NaCl). The hemolytic activity was related to protein concentration
and the HU50 against chicken erythrocytes was 0.91 μg/mL. 相似文献
3.
Amplified fragment length polymorphisms(AFLP) markers were developed to assess the genetic variation of populations and clones of Rhopilema esculentum Kishinouye(Scyphozoa,Rhizostomatidae).One hundred and seventy-nine loci from 56 individuals of two hatchery populations and two wild populations were genotyped with five primer combinations.The polymorphic ratio,Shannon’s diversity index and average heterozygosity were 70.3%,0.346 and 0.228 for the white hatchery population,74.3%,0.313,and 0.201 for the red hatchery population,79.3%,0.349,and 0.224 for the Jiangsu wild population,and 74.9%,0.328 and 0.210 for the Penglai wild population,respectively.Thus,all populations had a relatively high level of genetic diversity.A specific band was identified that could separate the white from the red hatchery population.There was 84.85% genetic differentiation within populations.Individual cluster analysis using unweighted pair-group method with arithmetic mean(UPGMA) suggested that hatchery populations and wild populations could be divided.For the hatchery populations,the white and red populations clustered separately;however,for the wild populations,Penglai and Jiangsu populations clustered together.The genetic diversity at the clone level was also determined.Our data suggest that there are relatively high genetic diversities within populations but low genetic differentiation between populations,which may be related to the long-term use of germplasm resources from Jiangsu Province for artificial seeding and releasing.These findings will benefit the artificial seeding and conservation of the germplasm resources. 相似文献
4.
Guoyan Ren Bafang Li Xue Zhao Yongliang Zhuang Mingyan Yan Hu Hou Xiukun Zhang Li Chen 《中国海洋大学学报(英文版)》2009,8(1):83-88
In order to select an optimum extraction method for the target glycoprotein (TGP) from jellyfish (Rhopilema esculentum) oral-arms, a high performance liquid chromatography (HPLC)-assay for the determination of the TGP was developed. Purified
target glycoprotein was taken as a standard glycoprotein. The results showed that the calibration curves for peak area plotted
against concentration for TGP were linear (r = 0.9984, y = 4.5895x+47.601) over concentrations ranging from 50 to 400 mgL-1. The mean extraction recovery was 97.84% (CV2.60%). The fractions
containing TGP were isolated from jellyfish (R. esculentum) oral-arms by four extraction methods: 1) water extraction (WE), 2) phosphate buffer solution (PBS) extraction (PE), 3) ultrasound-assisted
water extraction (UA-WE), 4) ultrasound-assisted PBS extraction (UA-PE). The lyophilized extract was dissolved in Milli-Q
water and analyzed directly on a short TSK-GEL G4000PWXL (7.8 mm×300 mm) column. Our results indicated that the UA-PE method
was the optimum extraction method selected by HPLC. 相似文献
5.
REN Guoyan) ) LI Bafang) * ZHAO Xue) ZHUANG Yongliang) YAN Mingyan) HOU Hu) ZHANG Xiukun) CHEN Li)) Food Bioengineering Department Henan University of Science Technology Luoyang P. R. China ) College of Food Science Engineering Ocean University of China Qingdao P. R. China 《中国海洋大学学报(英文版)》2009,8(1)
In order to select an optimum extraction method for the target glycoprotein (TGP) from jellyfish (Rhopilema esculentum) oralarms, a high performance liquid chromatography (HPLC)–assay for the determination of the TGP was developed. Purified target glycoprotein was taken as a standard glycoprotein. The results showed that the calibration curves for peak area plotted against concentration for TGP were linear (r = 0.9984, y = 4.5895x+47.601) over concentrations ranging from 50 to 400 mgL-1. The mean extraction... 相似文献
6.
This study aimed to optimize the purification of recombinant growth hormone from Paralichthys olivaceus. Recombinant flounder growth hormone (r-fGH) was expressed by Escherichia coli in form of inclusion body or as soluble protein under different inducing conditions. The inclusion body was renatured using two recovery methods, i.e., dilution and dialysis. Thereafter, the refolded protein was purified by Glutathione Sepharase 4B affinity chromatography and r-fGH was obtained by cleavage of thrombin. For soluble products, r-fGH was directly purified from the lysates by Glutathione Sepharase 4B affinity chromatography. ELISA-receptor assay demonstrated that despite its low receptor binding activity, the r-fGH purified from refolded inclusion body had a higher yield (2.605 mgL-1) than that from soluble protein (1.964 mgL-1). Of the tested recovery methods, addition of renaturing buffer (pH 8.5) into denatured inclusion body yielded the best recovery rate (17.9%). This work provided an optimized purification method for high recovery of r-fGH, thus contributing to the application of r-fGH to aquaculture. 相似文献