PubMed:10366732 JSONTXT

{"project":"Anatomy-MAT","denotations":[{"id":"T1","span":{"begin":400,"end":405},"obj":"Body_part"}],"attributes":[{"id":"A1","pred":"mat_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/MAT_0000021"}],"text":"Determination of the site of disulfide linkage between heavy and light chains of silk fibroin produced by Bombyx mori.\nThe analysis of fibroin secretion-deficient 'naked-pupa' mutant silkworms has suggested that the disulfide linkage between heavy (H) and light (L) chains of fibroin, produced by the silkworm, Bombyx mori, is essential in its efficient large-scale secretion from the posterior silk gland cells. However, the site of disulfide-linkage between H- and L-chains has not been determined. In this study, cysteine residues involved in the single disulfide linkage between H- and L-chains were identified as the twentieth residue from the carboxyl terminus of H-chain (Cys-c20) and Cys-172 of L-chain by sequencing of genomic clones and peptide analysis. Furthermore, Cys-c4 (fourth residue from the carboxyl terminus) and Cys-c1 at the carboxyl terminus of H-chain were shown to form an intramolecular disulfide bond."}

{"project":"silkworm_phenotype","denotations":[{"id":"T28","span":{"begin":703,"end":710},"obj":"Gene:693047"},{"id":"T27","span":{"begin":467,"end":474},"obj":"Gene:693047"},{"id":"T26","span":{"begin":590,"end":597},"obj":"Gene:693047"},{"id":"T22","span":{"begin":263,"end":264},"obj":"Gene:693047"},{"id":"T21","span":{"begin":670,"end":677},"obj":"Gene:693030"},{"id":"T20","span":{"begin":868,"end":875},"obj":"Gene:693030"},{"id":"T18","span":{"begin":583,"end":584},"obj":"Gene:693030"},{"id":"T17","span":{"begin":460,"end":461},"obj":"Gene:693030"},{"id":"T16","span":{"begin":249,"end":250},"obj":"Gene:693030"},{"id":"T15","span":{"begin":164,"end":174},"obj":"BMO_00587"},{"id":"T9","span":{"begin":557,"end":566},"obj":"Chemical:MESH:D004220"},{"id":"T8","span":{"begin":516,"end":524},"obj":"Chemical:MESH:D003545"},{"id":"T7","span":{"begin":434,"end":443},"obj":"Chemical:MESH:D004220"},{"id":"T6","span":{"begin":311,"end":322},"obj":"Species:7091"},{"id":"T5","span":{"begin":301,"end":309},"obj":"Species:7091"},{"id":"T4","span":{"begin":216,"end":225},"obj":"Chemical:MESH:D004220"},{"id":"T3","span":{"begin":183,"end":192},"obj":"Species:7091"},{"id":"T2","span":{"begin":106,"end":117},"obj":"Species:7091"},{"id":"T14","span":{"begin":913,"end":922},"obj":"Chemical:MESH:D004220"},{"id":"T13","span":{"begin":833,"end":836},"obj":"Chemical:MESH:D003545"},{"id":"T12","span":{"begin":778,"end":781},"obj":"Chemical:MESH:D003545"},{"id":"T11","span":{"begin":692,"end":695},"obj":"Chemical:MESH:D003545"},{"id":"T10","span":{"begin":679,"end":682},"obj":"Chemical:MESH:D003545"},{"id":"T1","span":{"begin":29,"end":38},"obj":"Chemical:MESH:D004220"}],"text":"Determination of the site of disulfide linkage between heavy and light chains of silk fibroin produced by Bombyx mori.\nThe analysis of fibroin secretion-deficient 'naked-pupa' mutant silkworms has suggested that the disulfide linkage between heavy (H) and light (L) chains of fibroin, produced by the silkworm, Bombyx mori, is essential in its efficient large-scale secretion from the posterior silk gland cells. However, the site of disulfide-linkage between H- and L-chains has not been determined. In this study, cysteine residues involved in the single disulfide linkage between H- and L-chains were identified as the twentieth residue from the carboxyl terminus of H-chain (Cys-c20) and Cys-172 of L-chain by sequencing of genomic clones and peptide analysis. Furthermore, Cys-c4 (fourth residue from the carboxyl terminus) and Cys-c1 at the carboxyl terminus of H-chain were shown to form an intramolecular disulfide bond."}

{"project":"silkworm","denotations":[{"id":"T1","span":{"begin":29,"end":38},"obj":"Chemical:MESH:D004220"},{"id":"T2","span":{"begin":106,"end":117},"obj":"Species:7091"},{"id":"T3","span":{"begin":183,"end":192},"obj":"Species:7091"},{"id":"T4","span":{"begin":216,"end":225},"obj":"Chemical:MESH:D004220"},{"id":"T5","span":{"begin":301,"end":309},"obj":"Species:7091"},{"id":"T6","span":{"begin":311,"end":322},"obj":"Species:7091"},{"id":"T7","span":{"begin":434,"end":443},"obj":"Chemical:MESH:D004220"},{"id":"T8","span":{"begin":516,"end":524},"obj":"Chemical:MESH:D003545"},{"id":"T9","span":{"begin":557,"end":566},"obj":"Chemical:MESH:D004220"},{"id":"T10","span":{"begin":679,"end":682},"obj":"Chemical:MESH:D003545"},{"id":"T11","span":{"begin":692,"end":695},"obj":"Chemical:MESH:D003545"},{"id":"T12","span":{"begin":778,"end":781},"obj":"Chemical:MESH:D003545"},{"id":"T13","span":{"begin":833,"end":836},"obj":"Chemical:MESH:D003545"},{"id":"T14","span":{"begin":913,"end":922},"obj":"Chemical:MESH:D004220"}],"text":"Determination of the site of disulfide linkage between heavy and light chains of silk fibroin produced by Bombyx mori.\nThe analysis of fibroin secretion-deficient 'naked-pupa' mutant silkworms has suggested that the disulfide linkage between heavy (H) and light (L) chains of fibroin, produced by the silkworm, Bombyx mori, is essential in its efficient large-scale secretion from the posterior silk gland cells. However, the site of disulfide-linkage between H- and L-chains has not been determined. In this study, cysteine residues involved in the single disulfide linkage between H- and L-chains were identified as the twentieth residue from the carboxyl terminus of H-chain (Cys-c20) and Cys-172 of L-chain by sequencing of genomic clones and peptide analysis. Furthermore, Cys-c4 (fourth residue from the carboxyl terminus) and Cys-c1 at the carboxyl terminus of H-chain were shown to form an intramolecular disulfide bond."}

{"project":"silkwormbase","denotations":[{"id":"T22","span":{"begin":263,"end":264},"obj":"Gene:693047"},{"id":"T26","span":{"begin":590,"end":597},"obj":"Gene:693047"},{"id":"T1","span":{"begin":29,"end":38},"obj":"Chemical:MESH:D004220"},{"id":"T10","span":{"begin":679,"end":682},"obj":"Chemical:MESH:D003545"},{"id":"T11","span":{"begin":692,"end":695},"obj":"Chemical:MESH:D003545"},{"id":"T12","span":{"begin":778,"end":781},"obj":"Chemical:MESH:D003545"},{"id":"T13","span":{"begin":833,"end":836},"obj":"Chemical:MESH:D003545"},{"id":"T14","span":{"begin":913,"end":922},"obj":"Chemical:MESH:D004220"},{"id":"T2","span":{"begin":106,"end":117},"obj":"Species:7091"},{"id":"T3","span":{"begin":183,"end":192},"obj":"Species:7091"},{"id":"T4","span":{"begin":216,"end":225},"obj":"Chemical:MESH:D004220"},{"id":"T5","span":{"begin":301,"end":309},"obj":"Species:7091"},{"id":"T6","span":{"begin":311,"end":322},"obj":"Species:7091"},{"id":"T7","span":{"begin":434,"end":443},"obj":"Chemical:MESH:D004220"},{"id":"T8","span":{"begin":516,"end":524},"obj":"Chemical:MESH:D003545"},{"id":"T9","span":{"begin":557,"end":566},"obj":"Chemical:MESH:D004220"},{"id":"T15","span":{"begin":164,"end":174},"obj":"BMO_00587"},{"id":"T16","span":{"begin":249,"end":250},"obj":"Gene:693030"},{"id":"T17","span":{"begin":460,"end":461},"obj":"Gene:693030"},{"id":"T18","span":{"begin":583,"end":584},"obj":"Gene:693030"},{"id":"T20","span":{"begin":868,"end":875},"obj":"Gene:693030"},{"id":"T21","span":{"begin":670,"end":677},"obj":"Gene:693030"},{"id":"T27","span":{"begin":467,"end":474},"obj":"Gene:693047"},{"id":"T28","span":{"begin":703,"end":710},"obj":"Gene:693047"}],"text":"Determination of the site of disulfide linkage between heavy and light chains of silk fibroin produced by Bombyx mori.\nThe analysis of fibroin secretion-deficient 'naked-pupa' mutant silkworms has suggested that the disulfide linkage between heavy (H) and light (L) chains of fibroin, produced by the silkworm, Bombyx mori, is essential in its efficient large-scale secretion from the posterior silk gland cells. However, the site of disulfide-linkage between H- and L-chains has not been determined. In this study, cysteine residues involved in the single disulfide linkage between H- and L-chains were identified as the twentieth residue from the carboxyl terminus of H-chain (Cys-c20) and Cys-172 of L-chain by sequencing of genomic clones and peptide analysis. Furthermore, Cys-c4 (fourth residue from the carboxyl terminus) and Cys-c1 at the carboxyl terminus of H-chain were shown to form an intramolecular disulfide bond."}

{"project":"NCBITAXON","denotations":[{"id":"T1","span":{"begin":106,"end":117},"obj":"OrganismTaxon"},{"id":"T2","span":{"begin":170,"end":174},"obj":"OrganismTaxon"},{"id":"T3","span":{"begin":183,"end":192},"obj":"OrganismTaxon"},{"id":"T4","span":{"begin":301,"end":309},"obj":"OrganismTaxon"},{"id":"T5","span":{"begin":311,"end":322},"obj":"OrganismTaxon"}],"attributes":[{"id":"A1","pred":"db_id","subj":"T1","obj":"7091"},{"id":"A2","pred":"db_id","subj":"T2","obj":"96459"},{"id":"A3","pred":"db_id","subj":"T3","obj":"7091"},{"id":"A4","pred":"db_id","subj":"T4","obj":"7091"},{"id":"A5","pred":"db_id","subj":"T5","obj":"7091"}],"text":"Determination of the site of disulfide linkage between heavy and light chains of silk fibroin produced by Bombyx mori.\nThe analysis of fibroin secretion-deficient 'naked-pupa' mutant silkworms has suggested that the disulfide linkage between heavy (H) and light (L) chains of fibroin, produced by the silkworm, Bombyx mori, is essential in its efficient large-scale secretion from the posterior silk gland cells. However, the site of disulfide-linkage between H- and L-chains has not been determined. In this study, cysteine residues involved in the single disulfide linkage between H- and L-chains were identified as the twentieth residue from the carboxyl terminus of H-chain (Cys-c20) and Cys-172 of L-chain by sequencing of genomic clones and peptide analysis. Furthermore, Cys-c4 (fourth residue from the carboxyl terminus) and Cys-c1 at the carboxyl terminus of H-chain were shown to form an intramolecular disulfide bond."}

{"project":"Anatomy-UBERON","denotations":[{"id":"T1","span":{"begin":81,"end":85},"obj":"Body_part"},{"id":"T2","span":{"begin":170,"end":174},"obj":"Body_part"},{"id":"T3","span":{"begin":360,"end":365},"obj":"Body_part"},{"id":"T4","span":{"begin":385,"end":394},"obj":"Body_part"},{"id":"T5","span":{"begin":395,"end":405},"obj":"Body_part"}],"attributes":[{"id":"A1","pred":"uberon_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/UBERON_0012245"},{"id":"A2","pred":"uberon_id","subj":"T2","obj":"http://purl.obolibrary.org/obo/UBERON_0003143"},{"id":"A3","pred":"uberon_id","subj":"T3","obj":"http://purl.obolibrary.org/obo/UBERON_0002542"},{"id":"A4","pred":"uberon_id","subj":"T4","obj":"http://purl.obolibrary.org/obo/UBERON_0001353"},{"id":"A5","pred":"uberon_id","subj":"T5","obj":"http://purl.obolibrary.org/obo/UBERON_0011146"}],"text":"Determination of the site of disulfide linkage between heavy and light chains of silk fibroin produced by Bombyx mori.\nThe analysis of fibroin secretion-deficient 'naked-pupa' mutant silkworms has suggested that the disulfide linkage between heavy (H) and light (L) chains of fibroin, produced by the silkworm, Bombyx mori, is essential in its efficient large-scale secretion from the posterior silk gland cells. However, the site of disulfide-linkage between H- and L-chains has not been determined. In this study, cysteine residues involved in the single disulfide linkage between H- and L-chains were identified as the twentieth residue from the carboxyl terminus of H-chain (Cys-c20) and Cys-172 of L-chain by sequencing of genomic clones and peptide analysis. Furthermore, Cys-c4 (fourth residue from the carboxyl terminus) and Cys-c1 at the carboxyl terminus of H-chain were shown to form an intramolecular disulfide bond."}