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Strana 1 z 27 Výsledek
Molecular cloning and characterization of two soybean protein disulfide isomerases as molecular chaperones for seed storage proteins.
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Přihlášení Registrace
Protein disulfide isomerase family proteins play important roles in the folding of nascent polypeptides and the formation of disulfide bonds in the endoplasmic reticulum. In this study, we cloned two similar protein disulfide isomerase family genes from soybean leaf (Glycine max L. Merrill. cv
A novel plant protein disulfide isomerase family homologous to animal P5 - molecular cloning and characterization as a functional protein for folding of soybean seed-storage proteins.
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Přihlášení Registrace
The protein disulfide isomerase is known to play important roles in the folding of nascent polypeptides and in the formation of disulfide bonds in the endoplasmic reticulum (ER). In this study, we cloned a gene of a novel protein disulfide isomerase family from soybean leaf (Glycine max L. Merrill.
Accumulation of β-conglycinin in soybean cotyledon through the formation of disulfide bonds between α'- and α-subunits.
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Přihlášení Registrace
β-Conglycinin, one of the major soybean (Glycine max) seed storage proteins, is folded and assembled into trimers in the endoplasmic reticulum and accumulated into protein storage vacuoles. Prior experiments have used soybean β-conglycinin extracted using a reducing buffer containing a sulfhydryl
Molecular cloning and characterization of soybean protein disulfide isomerase family proteins with nonclassic active center motifs.
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Přihlášení Registrace
Protein disulfide isomerase (PDI) and other PDI family proteins are members of the thioredoxin superfamily and are thought to play important roles in disulfide bond formation and isomerization in the endoplasmic reticulum (ER). The exact functions of PDI family proteins in plants remain unknown. In
Disulfide bond formation activity of soybean quiescin sulfhydryl oxidase.
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Přihlášení Registrace
Multiple enzymatic systems can catalyse protein disulfide bond formation in the endoplasmic reticulum (ER) of eukaryotic cells. The enzyme quiescin sulfhydryl oxidase (QSOX) catalyses disulfide bond formation in unfolded proteins via the reduction of oxygen. We found two QSOX homologues in the
Auxin-Modulated Protein Disulfide-Thiol-Interchange Activity from Soybean Plasma Membranes.
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The renaturation of scrambled (oxidized and inactive) RNase A is catalyzed by soybean (Glycine max cv Williams 82) plasma membranes. The catalysis is stimulated by the auxin herbicide 2,4-dichlorophenoxyacetic acid or by the natural auxin indole-3-acetic acid. The inactive auxin analog,
Purification and characterization of protein disulfide isomerase from soybean.
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Přihlášení Registrace
Protein disulfide isomerase (PDI), which catalyses the folding of newly synthesized or denatured proteins through correct disulfide formation, was purified from soybean (Glycine max). The enzyme was purified 12,000-fold over crude extracts to apparent homogeneity in six purification steps: 60-70%
Use of Tetraethylthiuram Disulfide to Discriminate between Alternative Respiration and Lipoxygenase.
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Mitochondria from axes of Glycine max (L.) Merr. cv. Chippewa 64 seedlings purified on discontinuous Percoll gradients exhibited classical cyanide-resistant respiration. These mitochondria also possessed lipoxygenase activity, as determined by O(2) uptake in the presence of 0.8 millimolar linoleic
Protein disulfide isomerase family proteins involved in soybean protein biogenesis.
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Přihlášení Registrace
Protein disulfide isomerase family proteins are known to play important roles in the folding of nascent polypeptides and the formation of disulfide bonds in the endoplasmic reticulum. In this study, we cloned two similar protein disulfide isomerase family genes from soybean leaf (Glycine max L.
Complexation of bovine beta-lactoglobulin with 11S protein fractions of soybean (Glycine max) and sesame (Sesamum indicum).
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Beta-lactoglobulin (beta-Lg) comprises 50% of the whey component of bovine milk. Protein-protein interactions between bovine beta-Lg and 11S protein fractions of soybean and sesame were investigated by turbidity, solubility behaviour and by evaluation of functional properties in the mixed systems.
SBTX, a new toxic protein distinct from soyatoxin and other toxic soybean [Glycine max] proteins, and its inhibitory effect on Cercospora sojina growth.
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SBTX, a novel toxin from soybean, was purified by ammonium sulfate fractionation followed by chromatographic steps DEAE-Cellulose, CM-Sepharose and Superdex 200 HR fast-protein liquid chromatography (FPLC). Lethality of SBTX to mice (LD(50) 5.6 mg/kg) was used as parameter in the purification steps.
Thermally induced structural changes in glycinin, the 11S globulin of soya bean (Glycine max)--an in situ spectroscopic study.
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The thermal denaturation behaviour of glycinin solutions has been studied in situ as a function of ionic strength using various spectroscopic methods. Changes in secondary structure occurred at temperatures above 60 degrees C, well before the onset of gelation. Even after heating to 95 degrees C,
Redox regulation of a soybean tyrosine-specific protein phosphatase.
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Plant protein tyrosine phosphatases (PTPs) are important in regulating cellular responses to redox change through their reversible inactivation under oxidative conditions. Studies on the soybean (Glycine max) GmPTP have shown that, compared with its mammalian counterparts, the plant enzyme is
Analysis of a ferric leghemoglobin reductase from cowpea (Vigna unguiculata) root nodules.
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Ferric leghemoglobin reductase (FLbR), an enzyme reducing ferric leghemoglobin (Lb) to ferrous Lb, was purified from cowpea (Vigna unguiculata) root nodules by sequential chromatography on hydroxylapatite followed by Mono-Q HR5/5 FPLC and Sephacryl S-200 gel filtration. The purified cowpea FLbR had
Purification and characterization of mRNA from soybean seeds. Identification of glycinin and beta-conglycinin precursors.
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Poly(A)-rich RNA was isolated from developing soybean seeds (Glycine max (L.) Merr.) and fractionated on linear log sucrose gradients. Two major fractions sedimenting at 18 S and 20 S were separated and then purified by further sucrose gradient fractionation. Both fractions were active as messengers
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