{"title":"Aldosine, an Acid Hydrolysis Product from the Aldol Cross-link of Bovine Elastin and Collagen","authors":"K. Suyama, F. Nakamura","doi":"10.1271/BBB1961.55.3147","DOIUrl":"https://doi.org/10.1271/BBB1961.55.3147","url":null,"abstract":"","PeriodicalId":7729,"journal":{"name":"Agricultural and biological chemistry","volume":"23 1","pages":"3147-3149"},"PeriodicalIF":0.0,"publicationDate":"1991-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"78183047","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pyrazinamide is a strong inhibitor of aminocarboxymuconate semialdehyde decarboxylase (ACMSDase; EC 4.1.1.45) in vivo,1] which activity is thought to be critical in tryptophan-nicotinamide conversion.2 ~ 5) I reported that an intraperitoneal injection of pyrazinamide to rats fed with a nicotinic acid-free and 20% casein diet greatly increased urinary excretion of nicotinamide and its catabolic metabolites such as A^-methylnicotinamide (MNA), ^V 1-methyl-2-pyridone-5-carboxamide (2-Py), and Table I. Composition of Diets 3111
{"title":"Effects of Dietary Pyrazinamide on the Growth of Weanling Rats Fed with a Nicotinic Acid-free and Tryptophan-limited Diet","authors":"K. Shibata","doi":"10.1271/BBB1961.55.3111","DOIUrl":"https://doi.org/10.1271/BBB1961.55.3111","url":null,"abstract":"Pyrazinamide is a strong inhibitor of aminocarboxymuconate semialdehyde decarboxylase (ACMSDase; EC 4.1.1.45) in vivo,1] which activity is thought to be critical in tryptophan-nicotinamide conversion.2 ~ 5) I reported that an intraperitoneal injection of pyrazinamide to rats fed with a nicotinic acid-free and 20% casein diet greatly increased urinary excretion of nicotinamide and its catabolic metabolites such as A^-methylnicotinamide (MNA), ^V 1-methyl-2-pyridone-5-carboxamide (2-Py), and Table I. Composition of Diets 3111","PeriodicalId":7729,"journal":{"name":"Agricultural and biological chemistry","volume":"30 1","pages":"3111-3112"},"PeriodicalIF":0.0,"publicationDate":"1991-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"73557036","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 1991-12-01DOI: 10.1080/00021369.1991.10860156
K. Dekker, H. Yamagata, K. Sakaguchi, S. Udaka
{"title":"Production of ThermostableClostridium thermohydrosulfuricumXylose Isomerase inBacillus brevis","authors":"K. Dekker, H. Yamagata, K. Sakaguchi, S. Udaka","doi":"10.1080/00021369.1991.10860156","DOIUrl":"https://doi.org/10.1080/00021369.1991.10860156","url":null,"abstract":"","PeriodicalId":7729,"journal":{"name":"Agricultural and biological chemistry","volume":"35 4","pages":"2993-2998"},"PeriodicalIF":0.0,"publicationDate":"1991-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"91419766","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Seasonal changes of oligofructans, sucrose, glucose, and fructose contents in the various tissues of Lycoris radiata were followed by HPLC analyses. Oligofructans were found in all tissues except the scape, where large and nearly equal amounts of glucose and fructose were present. At the sprouting stage, oligofructans in the bulb greatly decreased with increases of both fructose content and β-fructofuranosidase activity. The bulb enzyme responsible for the fructan breakdown was a fructan exohydrolase that was inactive against sucrose, and the scape tissue contained a β-fructofuranosidase (EC 3.2.2.26) highly active toward sucrose. These results show a role of the accumulated fructans as an energy source for sprouting of the scape during the non-photosynthetic stage, the energy probably being supplied as sucrose.
{"title":"Fructan Mobilization and the Involvement of Two β-Fructofuranosidases in Lycoris radiata Sprouting","authors":"Y. Nagamatsu, M. Yahata, C. Hatanaka","doi":"10.1271/BBB1961.55.3091","DOIUrl":"https://doi.org/10.1271/BBB1961.55.3091","url":null,"abstract":"Seasonal changes of oligofructans, sucrose, glucose, and fructose contents in the various tissues of Lycoris radiata were followed by HPLC analyses. Oligofructans were found in all tissues except the scape, where large and nearly equal amounts of glucose and fructose were present. At the sprouting stage, oligofructans in the bulb greatly decreased with increases of both fructose content and β-fructofuranosidase activity. The bulb enzyme responsible for the fructan breakdown was a fructan exohydrolase that was inactive against sucrose, and the scape tissue contained a β-fructofuranosidase (EC 3.2.2.26) highly active toward sucrose. These results show a role of the accumulated fructans as an energy source for sprouting of the scape during the non-photosynthetic stage, the energy probably being supplied as sucrose.","PeriodicalId":7729,"journal":{"name":"Agricultural and biological chemistry","volume":"33 1","pages":"3091-3095"},"PeriodicalIF":0.0,"publicationDate":"1991-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"90404462","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
K. Kobayashi, T. Kamakura, T. Tanaka, I. Yamaguchi, T. Endō
duction of BS-deaminase (aminohydrolase, EC 3.5.4.23), which converted BS to an inactive derivative. Because of the broad spectrum of activity of blasticidin S, this antibioticresistance phenotype could be useful as a selection marker in genetic manipulation of both prokaryotic and eukaryotic cells. To this end, we obtained a plasmid pBSR8 (10.5kb) that encodes BS-deaminase. We describe the nucleotide sequence of the bsr gene, the determinant of the BS resistance, and compare the derived amino acid sequence with the N-terminal sequence of the enzyme purified from a resistant transformant. Cloning experiments using host vector systems of Bacillus subtilis and Escherichia coli and analyses of the recombinant plasmids located the bsr gene in the 1.5-kb EcoKl to
{"title":"Nucleotide sequence of the bsr gene and N-terminal amino acid sequence of blasticidin S deaminase from blasticidin S resistant Escherichia coli TK121.","authors":"K. Kobayashi, T. Kamakura, T. Tanaka, I. Yamaguchi, T. Endō","doi":"10.1271/BBB1961.55.3155","DOIUrl":"https://doi.org/10.1271/BBB1961.55.3155","url":null,"abstract":"duction of BS-deaminase (aminohydrolase, EC 3.5.4.23), which converted BS to an inactive derivative. Because of the broad spectrum of activity of blasticidin S, this antibioticresistance phenotype could be useful as a selection marker in genetic manipulation of both prokaryotic and eukaryotic cells. To this end, we obtained a plasmid pBSR8 (10.5kb) that encodes BS-deaminase. We describe the nucleotide sequence of the bsr gene, the determinant of the BS resistance, and compare the derived amino acid sequence with the N-terminal sequence of the enzyme purified from a resistant transformant. Cloning experiments using host vector systems of Bacillus subtilis and Escherichia coli and analyses of the recombinant plasmids located the bsr gene in the 1.5-kb EcoKl to","PeriodicalId":7729,"journal":{"name":"Agricultural and biological chemistry","volume":"7 1","pages":"3155-7"},"PeriodicalIF":0.0,"publicationDate":"1991-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"87598323","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 1991-12-01DOI: 10.1080/00021369.1991.10860054
M. Kimura, K. Hasegawa, H. Takamura, T. Matoba
The interesterification of triacylglycerol with fatty acid was done to prepare triacylglycerol molecular species. Optimum operating conditions for the interesterification using a 1,3-positional specific endocellular lipase from Rhizopus japonicus NR400 in a batch system were investigated. The reaction was done at 40°C for 5 hr in the following system: Trioleoylglycerol-palmitic acid = 1:3.5 (mol/mol), 10 ml n-hexane/g trioleoylglycerol, and 2500 units of enzyme/g trioleoylglycerol. Under these conditions, the content of palmitoyl groups in 1,3-positions of triacylglycerol was about 60 mol%. Additional interesterification (2-cycle reaction) using palmitic acid and the novel triacylglycerol prepared by one-step interesterification (1-cycle reaction) resulted in a preparation of highly pure 1,3-dipalmitoyl-2-oleoylglycerol.
通过脂肪酸与三酰基甘油的酯化反应制备了三酰基甘油分子种。以日本根霉NR400为原料，研究了1,3位置特异性细胞内脂肪酶在间歇式体系中酯化的最佳操作条件。反应条件为:三油基甘油-棕榈酸= 1:3.5 (mol/mol)，正己烷10 ml /三油基甘油，酶2500单位/g三油基甘油，反应温度40℃，反应时间5小时。在此条件下，三酰甘油中1,3位棕榈酰基的含量约为60 mol%。利用棕榈酸和一步酯化反应(1周期反应)制备的新型三酰甘油进行进一步的酯化反应(2周期反应)，得到了高纯度的1,3-二棕榈酰-2-油基甘油。
{"title":"Preparation of Triacylglycerol Molecular Species by Interesterification Using Endocellular Lipase in n-Hexane","authors":"M. Kimura, K. Hasegawa, H. Takamura, T. Matoba","doi":"10.1080/00021369.1991.10860054","DOIUrl":"https://doi.org/10.1080/00021369.1991.10860054","url":null,"abstract":"The interesterification of triacylglycerol with fatty acid was done to prepare triacylglycerol molecular species. Optimum operating conditions for the interesterification using a 1,3-positional specific endocellular lipase from Rhizopus japonicus NR400 in a batch system were investigated. The reaction was done at 40°C for 5 hr in the following system: Trioleoylglycerol-palmitic acid = 1:3.5 (mol/mol), 10 ml n-hexane/g trioleoylglycerol, and 2500 units of enzyme/g trioleoylglycerol. Under these conditions, the content of palmitoyl groups in 1,3-positions of triacylglycerol was about 60 mol%. Additional interesterification (2-cycle reaction) using palmitic acid and the novel triacylglycerol prepared by one-step interesterification (1-cycle reaction) resulted in a preparation of highly pure 1,3-dipalmitoyl-2-oleoylglycerol.","PeriodicalId":7729,"journal":{"name":"Agricultural and biological chemistry","volume":"2006 1","pages":"3039-3043"},"PeriodicalIF":0.0,"publicationDate":"1991-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"83045361","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Germano Cord Neto, Y. Kono, H. Hyakutake, Manabu Watanabe, Yoshikatsu Suzuki, A. Sakurai
As has been reported, antifungal or antibacterial substances such as momilactone,1* oryzalexin23) and oxygen- containing unsaturated fatty acids,4'5) and oryzalide6'7) have been isolated from cultivated rice plants as self-defense substances against microbial infection, i.e., Pyri-cularia and Xanthbmonascampestris, pv. oryzae. Somereports have demonstrated the resistance of wild rice species to P. oryzae8) and X. campestris,9) which are causal agents of rice blast and bacterial leaf blight disease, respectively. The isolation and identification of the antimicrobial substances in wild rice species, however, have yet been cultivated varieties and wild rice species based on a quantitative or qualitative analysis of their antimicrobial substances. Weselected Oryza officinalis, W0002, as a wild rice species resistant to rice blast disease,8) and isolated and identified ( - )-jasmonic acid as an antifungal substance from the leaves.
{"title":"Isolation and Identification of (-)-Jasmonic Acid from Wild Rice, Oryza officinalis, as an Antifungal Substance.","authors":"Germano Cord Neto, Y. Kono, H. Hyakutake, Manabu Watanabe, Yoshikatsu Suzuki, A. Sakurai","doi":"10.1271/BBB1961.55.3097","DOIUrl":"https://doi.org/10.1271/BBB1961.55.3097","url":null,"abstract":"As has been reported, antifungal or antibacterial substances such as momilactone,1* oryzalexin23) and oxygen- containing unsaturated fatty acids,4'5) and oryzalide6'7) have been isolated from cultivated rice plants as self-defense substances against microbial infection, i.e., Pyri-cularia and Xanthbmonascampestris, pv. oryzae. Somereports have demonstrated the resistance of wild rice species to P. oryzae8) and X. campestris,9) which are causal agents of rice blast and bacterial leaf blight disease, respectively. The isolation and identification of the antimicrobial substances in wild rice species, however, have yet been cultivated varieties and wild rice species based on a quantitative or qualitative analysis of their antimicrobial substances. Weselected Oryza officinalis, W0002, as a wild rice species resistant to rice blast disease,8) and isolated and identified ( - )-jasmonic acid as an antifungal substance from the leaves.","PeriodicalId":7729,"journal":{"name":"Agricultural and biological chemistry","volume":"3 1","pages":"3097-3098"},"PeriodicalIF":0.0,"publicationDate":"1991-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"84208301","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
To understand the mechanism by which gamma-polyglutamic acid (gamma-PGA) in the sticky material of natto was synthesized, we purified the gamma-glutamyltranspeptidase (gamma-GTP) (EC 2.3.2.2) from the culture broth of Bacillus subtilis (natto) to homogeneity. gamma-GTP was composed of two subunits with molecular weight of 45,000 and 22,000. The N-terminal amino acid sequence of light subunit was homologous with that of gamma-GTP from Escherichia coli. The optimum pH and temperature of activity were 8.5 and 60 degrees C. The enzyme was inactivated by incubation for 15 min at pH 8.0 and 55 degrees C, but little loss of the activity was detected at 40 degrees C. gamma-GTP used glutamine as a gamma-glutamyl donor and acceptor for gamma-PGA synthesis. Dipeptides were better gamma-glutamyl acceptors than free amino acids.
{"title":"Purification and properties of gamma-glutamyltranspeptidase from Bacillus subtilis (natto).","authors":"Y. Ogawa, H. Hosoyama, M. Hamano, H. Motai","doi":"10.1271/BBB1961.55.2971","DOIUrl":"https://doi.org/10.1271/BBB1961.55.2971","url":null,"abstract":"To understand the mechanism by which gamma-polyglutamic acid (gamma-PGA) in the sticky material of natto was synthesized, we purified the gamma-glutamyltranspeptidase (gamma-GTP) (EC 2.3.2.2) from the culture broth of Bacillus subtilis (natto) to homogeneity. gamma-GTP was composed of two subunits with molecular weight of 45,000 and 22,000. The N-terminal amino acid sequence of light subunit was homologous with that of gamma-GTP from Escherichia coli. The optimum pH and temperature of activity were 8.5 and 60 degrees C. The enzyme was inactivated by incubation for 15 min at pH 8.0 and 55 degrees C, but little loss of the activity was detected at 40 degrees C. gamma-GTP used glutamine as a gamma-glutamyl donor and acceptor for gamma-PGA synthesis. Dipeptides were better gamma-glutamyl acceptors than free amino acids.","PeriodicalId":7729,"journal":{"name":"Agricultural and biological chemistry","volume":"28 1","pages":"2971-7"},"PeriodicalIF":0.0,"publicationDate":"1991-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"84218391","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
S. Esaki, T. Goda, S. Takase, N. Sugiyama, S. Kamiya
To investigate the inhibitory potency of phloretin 2′-O-β-l-glycodides, phloretin 2′-O-(6-deoxy-β-l-galactoside) (1), -2′-O-(6-deoxy-β-l-galactoside) (2) and -2′-O-β-l-glucoside (3) were syn-thesized. The appropriate phloracetophenone 4′-O-β-l-glycosides were coupled with p-hydroxy-benzaldehyde in aq. alkali to yield the respective chalcone glycosides, which were catalytically hydrogenated to give 1–3.Compounds 1–3 as well as phloretin 2′-O-(6-deoxy-α-l-mannopyranoside) (glycyphyllin) each exhibited dose-dependent inhibition of 3-O-methyl-d-glucose-evoked ΔPD (transmural potential difference), using the everted jejunal segment of rats. A kinetic study revealed that the mode of action of 1–3 was non-conpetitive and that their Ki values were more than 400 times smaller than the Km value, indicating that they possess strong inhibitory potency toward the Na+ co-transporter.
为考察根皮素2′- o -β-l-糖苷的抑制作用，合成了根皮素2′- o -(6-脱氧-β-l-半乳糖苷)(1)、2′- o -(6-脱氧-β-l-半乳糖苷)(2)和2′- o -β-l-糖苷(3)。适当的苯乙酮4′-O-β-l-糖苷与对羟基苯甲醛在水溶液中偶联得到相应的查尔酮糖苷，催化加氢得到1-3。化合物1-3和根皮素2 ' - o -(6-脱氧-α-l-甘露糖吡喃苷)(glyphyllin)对3- o -甲基-d-葡萄糖诱导的ΔPD(跨壁电位差)均表现出剂量依赖性抑制作用。动力学研究表明，1-3的作用方式是非竞争性的，其Ki值比Km值小400倍以上，表明它们对Na+共转运体具有较强的抑制作用。
{"title":"Synthesis of Phloretin 2'-O-β-L-Glycosides and Their Inhibitory Action against Sugar Transport in Rat Small Intestine","authors":"S. Esaki, T. Goda, S. Takase, N. Sugiyama, S. Kamiya","doi":"10.1271/BBB1961.55.2855","DOIUrl":"https://doi.org/10.1271/BBB1961.55.2855","url":null,"abstract":"To investigate the inhibitory potency of phloretin 2′-O-β-l-glycodides, phloretin 2′-O-(6-deoxy-β-l-galactoside) (1), -2′-O-(6-deoxy-β-l-galactoside) (2) and -2′-O-β-l-glucoside (3) were syn-thesized. The appropriate phloracetophenone 4′-O-β-l-glycosides were coupled with p-hydroxy-benzaldehyde in aq. alkali to yield the respective chalcone glycosides, which were catalytically hydrogenated to give 1–3.Compounds 1–3 as well as phloretin 2′-O-(6-deoxy-α-l-mannopyranoside) (glycyphyllin) each exhibited dose-dependent inhibition of 3-O-methyl-d-glucose-evoked ΔPD (transmural potential difference), using the everted jejunal segment of rats. A kinetic study revealed that the mode of action of 1–3 was non-conpetitive and that their Ki values were more than 400 times smaller than the Km value, indicating that they possess strong inhibitory potency toward the Na+ co-transporter.","PeriodicalId":7729,"journal":{"name":"Agricultural and biological chemistry","volume":"1988 1","pages":"2855-2860"},"PeriodicalIF":0.0,"publicationDate":"1991-11-23","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"82286292","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Comparative immunochemical studies of exocellular glucuronoxylomannans of several species of the genera Tremella and Cryptococcus were done with rabbit antisera prepared to two yeast-form strains (T7 and T19) of Tremella fuciformis Berk. Quantitative precipitin test showed that glucuronoxylomannans of Cryptococcus were precipitated with the antiserum to T. fuciformis T7 but not with the antiserum to T. fuciformis T19. In contrast, glucuronoxylomannans of Tremella are reactive with antiserum to T. fuciformis T19. Hapten inhibition tests and structural analyses of glucuronoxylomannans indicated that presence or absence of β-(1→2)-linked d-xylose short chain in glucuronoxylomannan may contribute to the serological difference among species of Tremella and Cryptococcus.
{"title":"Immunochemical studies of exocellular polysaccharides of Tremella and Cryptococcus","authors":"Y. Sone, A. Misaki, M. Torii","doi":"10.1271/BBB1961.55.2683","DOIUrl":"https://doi.org/10.1271/BBB1961.55.2683","url":null,"abstract":"Comparative immunochemical studies of exocellular glucuronoxylomannans of several species of the genera Tremella and Cryptococcus were done with rabbit antisera prepared to two yeast-form strains (T7 and T19) of Tremella fuciformis Berk. Quantitative precipitin test showed that glucuronoxylomannans of Cryptococcus were precipitated with the antiserum to T. fuciformis T7 but not with the antiserum to T. fuciformis T19. In contrast, glucuronoxylomannans of Tremella are reactive with antiserum to T. fuciformis T19. Hapten inhibition tests and structural analyses of glucuronoxylomannans indicated that presence or absence of β-(1→2)-linked d-xylose short chain in glucuronoxylomannan may contribute to the serological difference among species of Tremella and Cryptococcus.","PeriodicalId":7729,"journal":{"name":"Agricultural and biological chemistry","volume":"12 1","pages":"2683-2686"},"PeriodicalIF":0.0,"publicationDate":"1991-11-23","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"77903018","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
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