Pub Date : 2000-06-30DOI: 10.11416/KONTYUSHIGEN1930.69.169
A. R. Reddy, K. Chaitanya, D. Sundar
Waters stress-induced responses in the activities of superoxide dismutase (SOD), catalase (CAT), ascrobate peroxidase (APX) and peroxidase (POD) from three different genotypes (K-2, MR-2 and BC2-59) of mulberry (Morus alba L.) were determined. In response to water deficit, increases in the activities of SOD, CAT, APX and POD were observed in all the three genotypes. Progressive increase in the activities of the antioxidant enzymes was observed with decreasing leaf water potentials from -0.75 MPa to -2.25 MPa. However BC2-59 showed significantly higher activities of all the three antioxidant enzymes under low water regimes compared to those from K-2 and MR-2. The results clearly suggest that low leaf water potentials induce the antioxidant enzymes in all the three genotypes of mulberry. Our data indicate that the genotype BC2-59 has efficient antioxidant system among the three cultivars which could protect the oxidative damage caused due to water limited conditions.
{"title":"Water stress-mediated changes in antioxidant enzyme activities of mulberry (Morus alba L.)","authors":"A. R. Reddy, K. Chaitanya, D. Sundar","doi":"10.11416/KONTYUSHIGEN1930.69.169","DOIUrl":"https://doi.org/10.11416/KONTYUSHIGEN1930.69.169","url":null,"abstract":"Waters stress-induced responses in the activities of superoxide dismutase (SOD), catalase (CAT), ascrobate peroxidase (APX) and peroxidase (POD) from three different genotypes (K-2, MR-2 and BC2-59) of mulberry (Morus alba L.) were determined. In response to water deficit, increases in the activities of SOD, CAT, APX and POD were observed in all the three genotypes. Progressive increase in the activities of the antioxidant enzymes was observed with decreasing leaf water potentials from -0.75 MPa to -2.25 MPa. However BC2-59 showed significantly higher activities of all the three antioxidant enzymes under low water regimes compared to those from K-2 and MR-2. The results clearly suggest that low leaf water potentials induce the antioxidant enzymes in all the three genotypes of mulberry. Our data indicate that the genotype BC2-59 has efficient antioxidant system among the three cultivars which could protect the oxidative damage caused due to water limited conditions.","PeriodicalId":22665,"journal":{"name":"The journal of sericultural science of Japan","volume":"1 1","pages":"169-175"},"PeriodicalIF":0.0,"publicationDate":"2000-06-30","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"88126548","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 : 2000-06-30DOI: 10.11416/KONTYUSHIGEN1930.69.191
Rensuke Kanekatsu, E. Iizuka, K. Shirai, K. Kiguchi, K. Abe, A. Hachimori
Introduction Natural fibers have both desirable and undesirable properties. Silk is lustrous, well dyeable and heat-retaining. It absorbs and releases moisture quickly. Fbbroin also immobilizes enzymes (DEMURA and ASAKURA,1989), helps living cells multiply on it (MINOURA et al., 1995) and slowly diffuses medication (CHEN et al., 1990). Thus, silk is a promising material for a functional polymer as well as for clothes; however, it is inferior to another natural fiber, cotton, in some respects such as heat-resistance and friction resistance properties. Although cotton doesn't appear to be functional, it is tough and appears to be useful as a supporting material. This study has been carried out to determine the feasibility of a new material for textile fibers and functional substances by combining these two characteristic natural polymers: fibroin and cotton. Materials and Methods
天然纤维有理想的和不理想的特性。丝绸有光泽，可染性好，保温性好。它吸收和释放水分很快。Fbbroin还可以固定酶(DEMURA and ASAKURA,1989)，帮助活细胞在其上繁殖(MINOURA et al.， 1995)，缓慢扩散药物(CHEN et al.， 1990)。因此，丝绸是一种很有前途的功能性聚合物材料和服装材料;然而，它在耐热性和耐摩擦性能等某些方面不如另一种天然纤维——棉花。虽然棉花似乎没有功能，但它很坚韧，似乎是有用的支撑材料。本研究是为了确定一种纺织纤维和功能物质的新材料的可行性，将这两种具有特征的天然聚合物:丝素和棉花结合在一起。材料与方法
{"title":"Production and mechanical properties of fibroin-cellulose blended fiber","authors":"Rensuke Kanekatsu, E. Iizuka, K. Shirai, K. Kiguchi, K. Abe, A. Hachimori","doi":"10.11416/KONTYUSHIGEN1930.69.191","DOIUrl":"https://doi.org/10.11416/KONTYUSHIGEN1930.69.191","url":null,"abstract":"Introduction Natural fibers have both desirable and undesirable properties. Silk is lustrous, well dyeable and heat-retaining. It absorbs and releases moisture quickly. Fbbroin also immobilizes enzymes (DEMURA and ASAKURA,1989), helps living cells multiply on it (MINOURA et al., 1995) and slowly diffuses medication (CHEN et al., 1990). Thus, silk is a promising material for a functional polymer as well as for clothes; however, it is inferior to another natural fiber, cotton, in some respects such as heat-resistance and friction resistance properties. Although cotton doesn't appear to be functional, it is tough and appears to be useful as a supporting material. This study has been carried out to determine the feasibility of a new material for textile fibers and functional substances by combining these two characteristic natural polymers: fibroin and cotton. Materials and Methods","PeriodicalId":22665,"journal":{"name":"The journal of sericultural science of Japan","volume":"197 1","pages":"191-196"},"PeriodicalIF":0.0,"publicationDate":"2000-06-30","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"76057518","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 : 2000-06-30DOI: 10.11416/KONTYUSHIGEN1930.69.225
Yonghuang Jiang, Y. Banno, H. Fujii
The digestive juice of the larvae of the silkworm, Bombyx mori include many proteases. Some were isolated and characterized (EGUCHI and IWAMOTo, 1982; SASAKI and SUZUKI, 1982; KIDO et al., 1986; KoTANI et al., 1999), but their heterogeneity has not been investigated, for except one case (EGUCHI and YOSHITAKE, 1967). We purified an enzyme named as 35K protease from silkworm digestive juice (JIANG et al., 2000). This enzyme is a chymotrypsin-like protease and was inhibited by CI-8 (SHIRAI et al., 1997) in the larval hemolymph. During our investigation, we discovered polymorphism of the 35K protease from digestive juice of silkworm. In this paper, we focus on polymorphism and the mode of inheritance of 35K protease.
家蚕(Bombyx mori)幼虫的消化液含有许多蛋白酶。有些被分离出来并被鉴定(EGUCHI和IWAMOTo, 1982;SASAKI and SUZUKI, 1982;KIDO et al.， 1986;KoTANI et al.， 1999)，但除了一个案例(EGUCHI and YOSHITAKE, 1967)外，他们的异质性尚未被调查。我们从蚕的消化液中纯化了一种酶，命名为35K蛋白酶(JIANG等，2000)。这种酶是一种凝乳胰蛋白酶样蛋白酶，在幼虫血淋巴中被CI-8抑制(SHIRAI et al.， 1997)。在我们的调查中，我们发现了蚕消化液中35K蛋白酶的多态性。本文主要对35K蛋白酶的多态性及其遗传方式进行了研究。
{"title":"Genetic variant and inheritance of the 35K protease in digestive juice of silkworm, Bombyx mori","authors":"Yonghuang Jiang, Y. Banno, H. Fujii","doi":"10.11416/KONTYUSHIGEN1930.69.225","DOIUrl":"https://doi.org/10.11416/KONTYUSHIGEN1930.69.225","url":null,"abstract":"The digestive juice of the larvae of the silkworm, Bombyx mori include many proteases. Some were isolated and characterized (EGUCHI and IWAMOTo, 1982; SASAKI and SUZUKI, 1982; KIDO et al., 1986; KoTANI et al., 1999), but their heterogeneity has not been investigated, for except one case (EGUCHI and YOSHITAKE, 1967). We purified an enzyme named as 35K protease from silkworm digestive juice (JIANG et al., 2000). This enzyme is a chymotrypsin-like protease and was inhibited by CI-8 (SHIRAI et al., 1997) in the larval hemolymph. During our investigation, we discovered polymorphism of the 35K protease from digestive juice of silkworm. In this paper, we focus on polymorphism and the mode of inheritance of 35K protease.","PeriodicalId":22665,"journal":{"name":"The journal of sericultural science of Japan","volume":"15 1","pages":"225-227"},"PeriodicalIF":0.0,"publicationDate":"2000-06-30","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"79723200","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 : 2000-06-30DOI: 10.11416/KONTYUSHIGEN1930.69.197
N. Imai, S. Ali, N. El-Singaby, M. Iwanaga, S. Matsumoto, K. Iwabuchi, S. Maeda
A system of the baculovirus Bombyx mori nucleopolyhedrovirus (BmNPV) and the silkworm larvae, B. mori, was applied to analyze the potential use of the insect-specific toxin LghIT2 for improving the efficiency of recombinant baculoviruses for pest control. The LghIT2 gene, along with the signal sequence for secretion, was synthesized and transferred into the BmNPV genome to generate the recombinant virus BmLqhIT2. Larvae infected with BmLqhIT2 showed LqhIT2-specific symptoms at 48 h post injection (p. i.), stopped feeding at 60 h p. i., and became motionless by 84 h p. i. Particularly, the larvae infected with BmLghIT2 stopped moving 24 h earlier than those infected with BmAaIT, which expressed another insect-specific scorpion toxin AaIT. An N-terminal sequence and mass spectrometric analyses showed that BmLqhIT2 produced mature LghIT2. The present results suggest that LqhIT2 is more efficient than AaIT for improving the Insecticidal activity of baculoviruses.
采用家蚕杆状病毒核多角体病毒(BmNPV)和家蚕幼虫组成的系统，分析了昆虫特异性毒素LghIT2在提高重组杆状病毒防治害虫效率方面的潜在应用价值。合成LghIT2基因和分泌信号序列，并将其转移到BmNPV基因组中，生成重组病毒BmLqhIT2。感染BmLqhIT2的幼虫在注射后48 h (p. i.)出现lqhit2特异性症状，60 h停止进食，84 h静止不动，特别是感染BmLqhIT2的幼虫比感染表达另一种昆虫特异性蝎子毒素ait的BmAaIT早24 h停止运动。n端序列和质谱分析表明BmLqhIT2产生成熟的LghIT2。结果表明，LqhIT2比ait更能提高杆状病毒的杀虫活性。
{"title":"Insecticidal effects of a recombinant baculovirus expressing scorpion toxin LqhIT2","authors":"N. Imai, S. Ali, N. El-Singaby, M. Iwanaga, S. Matsumoto, K. Iwabuchi, S. Maeda","doi":"10.11416/KONTYUSHIGEN1930.69.197","DOIUrl":"https://doi.org/10.11416/KONTYUSHIGEN1930.69.197","url":null,"abstract":"A system of the baculovirus Bombyx mori nucleopolyhedrovirus (BmNPV) and the silkworm larvae, B. mori, was applied to analyze the potential use of the insect-specific toxin LghIT2 for improving the efficiency of recombinant baculoviruses for pest control. The LghIT2 gene, along with the signal sequence for secretion, was synthesized and transferred into the BmNPV genome to generate the recombinant virus BmLqhIT2. Larvae infected with BmLqhIT2 showed LqhIT2-specific symptoms at 48 h post injection (p. i.), stopped feeding at 60 h p. i., and became motionless by 84 h p. i. Particularly, the larvae infected with BmLghIT2 stopped moving 24 h earlier than those infected with BmAaIT, which expressed another insect-specific scorpion toxin AaIT. An N-terminal sequence and mass spectrometric analyses showed that BmLqhIT2 produced mature LghIT2. The present results suggest that LqhIT2 is more efficient than AaIT for improving the Insecticidal activity of baculoviruses.","PeriodicalId":22665,"journal":{"name":"The journal of sericultural science of Japan","volume":"15 1","pages":"197-205"},"PeriodicalIF":0.0,"publicationDate":"2000-06-30","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"73329243","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 : 2000-06-30DOI: 10.11416/KONTYUSHIGEN1930.69.215
C. Takabayashi, Kohkiti Hikobe, E. Miyazaki, T. Itsubo, Kuniko Nakamura
{"title":"Development of the reeling machines of three-dimensional type silk material “Silk Shell” and the production","authors":"C. Takabayashi, Kohkiti Hikobe, E. Miyazaki, T. Itsubo, Kuniko Nakamura","doi":"10.11416/KONTYUSHIGEN1930.69.215","DOIUrl":"https://doi.org/10.11416/KONTYUSHIGEN1930.69.215","url":null,"abstract":"","PeriodicalId":22665,"journal":{"name":"The journal of sericultural science of Japan","volume":"183 1","pages":"215-219"},"PeriodicalIF":0.0,"publicationDate":"2000-06-30","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"77176489","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 : 2000-06-30DOI: 10.11416/KONTYUSHIGEN1930.69.163
K. Ikeda, H. Saito, Shun Sato, T. Kodama
{"title":"Growth-inhibition effect of Streptomyces sp. 39L40C to mulberry twig blight pathogen, Fusarium lateritium f. sp. mori","authors":"K. Ikeda, H. Saito, Shun Sato, T. Kodama","doi":"10.11416/KONTYUSHIGEN1930.69.163","DOIUrl":"https://doi.org/10.11416/KONTYUSHIGEN1930.69.163","url":null,"abstract":"","PeriodicalId":22665,"journal":{"name":"The journal of sericultural science of Japan","volume":"23 1","pages":"163-168"},"PeriodicalIF":0.0,"publicationDate":"2000-06-30","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"76287968","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 : 2000-06-30DOI: 10.11416/KONTYUSHIGEN1930.69.221
T. Kako
{"title":"Dyeability of Chitosan-treated Tussah Silk Fabric by 1:1 Type Premetalized and 1:2 Type Premetalized Dyes","authors":"T. Kako","doi":"10.11416/KONTYUSHIGEN1930.69.221","DOIUrl":"https://doi.org/10.11416/KONTYUSHIGEN1930.69.221","url":null,"abstract":"","PeriodicalId":22665,"journal":{"name":"The journal of sericultural science of Japan","volume":"47 1","pages":"221-224"},"PeriodicalIF":0.0,"publicationDate":"2000-06-30","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"80402521","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 : 2000-04-28DOI: 10.11416/KONTYUSHIGEN1930.69.83
Jianyun Zhang, Longquan Huang, T. Hayakawa, H. Tsuge
{"title":"Response of the silkworm, Bombyx mori to the addition of pteroylglutamic acid in synthetic diet","authors":"Jianyun Zhang, Longquan Huang, T. Hayakawa, H. Tsuge","doi":"10.11416/KONTYUSHIGEN1930.69.83","DOIUrl":"https://doi.org/10.11416/KONTYUSHIGEN1930.69.83","url":null,"abstract":"","PeriodicalId":22665,"journal":{"name":"The journal of sericultural science of Japan","volume":"71 1","pages":"83-89"},"PeriodicalIF":0.0,"publicationDate":"2000-04-28","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"91200494","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 : 2000-04-28DOI: 10.11416/KONTYUSHIGEN1930.69.131
K. Shirai, Rensuke Kanekatsu, K. Kiguchi
{"title":"Carotenoids in the lipophorin of the sweet potato hornworm, Agrius convolvuli and the silkworm, Bombyx mori","authors":"K. Shirai, Rensuke Kanekatsu, K. Kiguchi","doi":"10.11416/KONTYUSHIGEN1930.69.131","DOIUrl":"https://doi.org/10.11416/KONTYUSHIGEN1930.69.131","url":null,"abstract":"","PeriodicalId":22665,"journal":{"name":"The journal of sericultural science of Japan","volume":"351 1","pages":"131-138"},"PeriodicalIF":0.0,"publicationDate":"2000-04-28","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"76581674","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 : 2000-04-28DOI: 10.11416/KONTYUSHIGEN1930.69.121
H. Arai, T. Okido, H. Fujii, H. Doira
Total esterase activity in the hemolymph of Bombyx mori was measured using a-naphthyl acetate as a substrate. It was low during the early fifth instar, then sharply increased at the spinning stage and stayed high throughout the pupal stage. One of the major hemolymph esterases of B. mori, previously named BesB (blood esterase B type), was purified from day 1 pupae to homogeneity using procedures such as procainamide hydrochloride affinity chromatography. BesB had an apparent molecular weight of 58,000 and an isoelectric point of 4.6. It was most active at pH 6-7, and was stable around pH 7 to 9. The sequence of N-terminal 28 amino acid residues was partially homologous to previously reported esterases isolated from the peach-potato aphid Myzus persicae. In kinetic parameters, there were no differences in Km values from four tested substrates, but there were differences in Vmax values. BesB had the highest sensitivity to paraoxon and diisopropyl f luorophosphate (DFP), and was moderately affected by eserin sulfate, phenylmethylsulf onyl fluoride (PMSF) and chloromercuribenzoic acid (pCMB). These results indicate that BesB is a carboxylesterase in hemolymph.
{"title":"Purification and characterization of a major esterase BesB from hemolymph of the silkworm Bombyx mori","authors":"H. Arai, T. Okido, H. Fujii, H. Doira","doi":"10.11416/KONTYUSHIGEN1930.69.121","DOIUrl":"https://doi.org/10.11416/KONTYUSHIGEN1930.69.121","url":null,"abstract":"Total esterase activity in the hemolymph of Bombyx mori was measured using a-naphthyl acetate as a substrate. It was low during the early fifth instar, then sharply increased at the spinning stage and stayed high throughout the pupal stage. One of the major hemolymph esterases of B. mori, previously named BesB (blood esterase B type), was purified from day 1 pupae to homogeneity using procedures such as procainamide hydrochloride affinity chromatography. BesB had an apparent molecular weight of 58,000 and an isoelectric point of 4.6. It was most active at pH 6-7, and was stable around pH 7 to 9. The sequence of N-terminal 28 amino acid residues was partially homologous to previously reported esterases isolated from the peach-potato aphid Myzus persicae. In kinetic parameters, there were no differences in Km values from four tested substrates, but there were differences in Vmax values. BesB had the highest sensitivity to paraoxon and diisopropyl f luorophosphate (DFP), and was moderately affected by eserin sulfate, phenylmethylsulf onyl fluoride (PMSF) and chloromercuribenzoic acid (pCMB). These results indicate that BesB is a carboxylesterase in hemolymph.","PeriodicalId":22665,"journal":{"name":"The journal of sericultural science of Japan","volume":"24 1","pages":"121-130"},"PeriodicalIF":0.0,"publicationDate":"2000-04-28","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"86445485","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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