| 499 matches found in 345 documents. Search time: 0.036 seconds. |
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| Title: The refolding , purification , and activity analysis of a rice Bowman-Birk inhibitor expressed in Escherichia coli .
| | Author: Li N Qu LJ Liu Y Li Q Gu H Chen Z | | Journal: Protein Expr . Purif . Citation: V : 15 ( 1 ) P : 99-104 Year: 1999 Type: ARTICLE | | Literature: oryza Field: abstract Doc ID: pub10024476 Accession (PMID): 10024476 | Matching Sentences:
[ Sen. 5, subscore: 1.00 ]: A putative rice trypsin/chymotrypsin inhibitor of the Bowman-Birk family , RBBI-8 of about 20 kDa , was expressed in Escherichia coli as a fusion protein bearing an N-terminal ( His ) 6 purification tag . The expressed recombinant protein , rRBBI-8 , is insoluble and accumulates as inclusion bodies . The insoluble protein was solubilized in 8 M urea under reducing environment and then refolded into its active conformation under optimized redox conditions . Strategies used to optimize yield and efficiency include selecting the redox system , increasing protein concentration during refolding by adding the denatured protein in a stepwise way , utilizing additives to prevent aggregation , and selecting buffer-exchanging conditions . A Ni-chelate affinity column was then employed to purify the renatured protein . rRBBI-8 shows strong inhibitory activity against trypsin and it can slightly inhibit chymotrypsin . In this study , a refolding and purification system was set up for this cysteine-rich recombinant protein expressed in a prokaryotic system .
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| Title: Isolation and characterization of the gene encoding the starch debranching enzyme limit dextrinase from germinating barley .
| | Author: Kristensen M Lok F Planchot V Svendsen I Leah R Svensson B | | Journal: Biochim . Biophys . Acta Citation: V : 1431 ( 2 ) P : 538-46 Year: 1999 Type: ARTICLE | | Literature: oryza Field: abstract Doc ID: pub10350630 Accession (PMID): 10350630 | Matching Sentences:
[ Sen. 8, subscore: 1.00 ]: The coding sequence is interrupted by 26 introns varying in length from 93 bp to 825 bp . The 27 exons vary in length from 53 bp to 197 bp . Southern blot analysis shows that the limit dextrinase gene is present as a single copy in the barley genome . Gene expression is high during germination and the steady state transcription level reaches a maximum at day 5 of germination . The deduced amino acid sequence corresponds to the protein sequence of limit dextrinase purified from germinating malt , as determined by automated N-terminal sequencing of tryptic fragments coupled with matrix assisted laser desorption mass spectrometry . The sequenced peptide fragments cover 70% of the entire protein sequence , which shows 62% and 77% identity to that of starch debranching enzymes from spinach and rice and 37% identity to Klebsiella pullulanase . Sequence alignment supports the multidomain architecture and identifies both secondary structure elements of the catalytic ( beta/alpha ) 8-barrel substrate , catalytic residues , and specificity associated motifs characteristic of members of the glycoside hydrolase family 13 which cleave alpha-1 , 6-glucosidic bonds . A remarkable distribution of the secondary structure elements to individual exons is observed .
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| Title: Localization of farnesyl diphosphate synthase in chloroplasts .
| | Author: Sanmiya K Ueno O Matsuoka M Yamamoto N | | Journal: Plant Cell Physiol .
Citation: V : 40 ( 3 ) P : 348-54 Year: 1999 Type: ARTICLE | | Literature: oryza Field: abstract Doc ID: pub10353221 Accession (PMID): 10353221 | Matching Sentences:
[ Sen. 4, subscore: 1.00 ]: The subcellular localization of plant farnesyl diphosphate synthase ( FPPS ) was examined . Immunocytochemical staining using anti-FPPS1 antibody followed by electron microscopy showed that FPPS1 was localized to chloroplasts of rice mesophyll cells . Subcellular fractions from wheat leaves were examined by immunoblot analysis . FPPS was detected in the chloroplast fraction in wheat , and was protected from proteolysis following trypsin treatment of chloroplasts . FPPS was also detected in the chloroplast fraction of a dicot plant , tobacco
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| Title: Nitrogen retention and plasma amino acids of adults who consumed isonitrogenous diets containing rice and milk or wheat versus their constituent amino acids .
| | Author: Clark HE Moon W-H Bailey LB Panemangelore M | | Journal: Am .
J Clin . Nutr . Citation: V : 29 ( 12 ) P : 1343-52 Year: 1976 Type: ARTICLE | | Literature: oryza Field: abstract Doc ID: pub1036663 Accession (PMID): 1036663 | Matching Sentences:
[ Sen. 4, subscore: 1.00 ]: Nitrogen retention and concentrations of plasma amino acids were compared when young adults consumed isonitrogenous diets containing proteins ( 3 . 0 g of N from rice plus 3 . 0 g of N from milk or 3 . 0 g of N from rice plus 3 . 0 g of N from wheat flour ) or mixtures of their constituent amino acids . Diets containing proteins induced greater nitrogen retention than did those containing corresponding amounts of amino acids in crystalline form , and the difference between the combinations of proteins was delineated more sharply . Concentrations of several amino acids were elevated by substituting crystalline amino acids for proteins , especially in postprandial plasma . Subjects responded differently to addition of the limiting amino acids , lysine and tryptophan , to the diets containing amino acids instead of rice plus wheat . Therefore , data obtained by means of combinations of cereals and by mixtures of their constituent amino acids can not always be used interchangeably .
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| Title: Molecular cloning and characterization of a cysteine-rich 16 . 6-kDa prolamin in rice seeds .
| | Author: Mitsukawa N Konishi R Uchiki M Masumura T Tanaka K | | Journal: Biosci . Biotechnol . Biochem . Citation: V : 63 ( 11 ) P : 1851-8 Year: 1999 Type: ARTICLE | | Literature: oryza Field: abstract Doc ID: pub10635550 Accession (PMID): 10635550 | Matching Sentences:
[ Sen. 2, subscore: 1.00 ]: An alcohol-soluble storage protein , a 16 . 6-kDa prolamin found in rice seeds , was purified from both the total protein body and purified type I protein body fractions . The partial amino acid sequences of three tryptic peptides generated from the purified polypeptide were analyzed . A part of the 16 . 6-kDa prolamin cDNA was amplified from developing seed mRNA by the reverse transcribed polymerase chain reaction using an oligo ( dT ) primer and a primer which was synthesized based on the partial amino acid sequence . The amplified product was used to isolate the full-length cDNA clone ( lambda RP16 ) from a developing seed cDNA library . The cDNA has an open reading frame encoding a hydrophobic polypeptide of 149 amino acids . The polypeptide was rich in glutamine ( 20 . 0% ) , cysteine ( 10 . 0% ) , and methionine ( 6 . 9% ) .
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Score: 3.00 |
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| Title: Identification of novel serine proteinase gene transcripts in the midguts of two tropical insect pests , Scirpophaga incertulas ( Wk . ) and Helicoverpa armigera ( Hb . ) .
| | Author: Mazumdar-Leighton S Babu CR Bennett J | | Journal: Insect Biochem . Mol . Biol . Citation: V : 30 ( 1 ) P : 57-68 Year: 2000 Type: ARTICLE | | Literature: oryza Field: abstract Doc ID: pub10646971 Accession (PMID): 10646971 | Matching Sentences:
[ Sen. 2, subscore: 1.00 ]: We have used RT PCR and 3RACE to identify diverse serine proteinase genes expressed in the midguts of the rice yellow stem borer ( Scirpophaga incertulas ) and Asian corn borer ( Helicoverpa armigera ) . The RT-PCR primers encoded the conserved regions around the active site histidine57 and serine195 of Drosophila melanogaster alpha trypsin , including aspartate189 of the specificity pocket . These primers amplified three transcripts ( SiP1-3 ) from midguts of S incertulas , and two transcripts ( HaP1-2 ) from midguts of H armigera . The five RT PCR products were sequenced to permit design of gene-specific forward primers for use with anchored oligo dT primers in 3RACE . Sequencing of the 3RACE products indicated that SiP1 , SiP2 and HaP1 encoded trypsin-like serine proteinases , while HaP2 encoded a chymotrypsin-like serine proteinases . The SiP3 transcript proved to be an abundant 960 nt mRNA encoding a trypsin-like protein in which the active site serine195 was replaced by aspartate .
[ Sen. 5, subscore: 1.00 ]: We have used RT PCR and 3RACE to identify diverse serine proteinase genes expressed in the midguts of the rice yellow stem borer ( Scirpophaga incertulas ) and Asian corn borer ( Helicoverpa armigera ) . The RT-PCR primers encoded the conserved regions around the active site histidine57 and serine195 of Drosophila melanogaster alpha trypsin , including aspartate189 of the specificity pocket . These primers amplified three transcripts ( SiP1-3 ) from midguts of S incertulas , and two transcripts ( HaP1-2 ) from midguts of H armigera . The five RT PCR products were sequenced to permit design of gene-specific forward primers for use with anchored oligo dT primers in 3RACE . Sequencing of the 3RACE products indicated that SiP1 , SiP2 and HaP1 encoded trypsin-like serine proteinases , while HaP2 encoded a chymotrypsin-like serine proteinases . The SiP3 transcript proved to be an abundant 960 nt mRNA encoding a trypsin-like protein in which the active site serine195 was replaced by aspartate . The possible functions of this unusual protein are discussed .
[ Sen. 6, subscore: 1.00 ]: The RT-PCR primers encoded the conserved regions around the active site histidine57 and serine195 of Drosophila melanogaster alpha trypsin , including aspartate189 of the specificity pocket . These primers amplified three transcripts ( SiP1-3 ) from midguts of S incertulas , and two transcripts ( HaP1-2 ) from midguts of H armigera . The five RT PCR products were sequenced to permit design of gene-specific forward primers for use with anchored oligo dT primers in 3RACE . Sequencing of the 3RACE products indicated that SiP1 , SiP2 and HaP1 encoded trypsin-like serine proteinases , while HaP2 encoded a chymotrypsin-like serine proteinases . The SiP3 transcript proved to be an abundant 960 nt mRNA encoding a trypsin-like protein in which the active site serine195 was replaced by aspartate . The possible functions of this unusual protein are discussed .
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| Title: Characterizing rice lesion mimic mutants and identifying a mutant with broad-spectrum resistance to rice blast and bacterial blight .
| | Author: Yin Z Chen J Zeng L Goh M Leung H Khush GS Wang GL .
| | Journal: Mol .
Plant Microbe Interact .
Citation: V : 13 ( 8 ) P : 869-76 Year: 2000 Type: ARTICLE | | Literature: oryza Field: abstract Doc ID: pub10939258 Accession (PMID): 10939258 | Matching Sentences:
[ Sen. 5, subscore: 1.00 ]: Many plant mutants develop spontaneous lesions that resemble disease symptoms in the absence of pathogen attack . In several pathosystems , lesion mimic mutations have been shown to be involved in programmed cell death , which in some instances leads to enhanced disease resistance to multiple pathogens . We investigated the relationship between spontaneous cell death and disease resistance in rice with nine mutants with a range of lesion mimic phenotypes . All nine mutations are controlled by recessive genes and some of these mutants have stunted growth and other abnormal characteristics . The lesion mimics that appeared on the leaves of these mutants were caused by cell death as measured by trypan blue staining . Activation of six defense-related genes was observed in most of the mutants when the mimic lesions developed . Four mutants exhibited significant enhanced resistance to rice blast One of the mutants , spl11 , confers non-race-specific resistance not only to blast but also to bacterial blight . The level of resistance in the spl11 mutant to the two pathogens correlates with the defense-related gene expression and lesion development on the leaves . The results suggest that some lesion mimic mutations in rice may be involved in disease resistance , and cloning of these genes may provide a clue to developing broad-spectrum resistance to diverse pathogens .
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Score: 2.00 |
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| Title: The maize major allergen , which is responsible for food-induced allergic reactions , is a lipid transfer protein .
| | Author: Pastorello EA Farioli L Pravettoni V Ispano M Scibola E Trambaioli C Giuffrida MG Ansaloni R Godovac-Zimmermann J Conti A Fortunato D Ortolani C | | Journal: J Allergy Clin . Immunol . Citation: V : 106 ( 4 ) P : 744-51 Year: 2000 Type: ARTICLE | | Literature: oryza Field: abstract Doc ID: pub11031346 Accession (PMID): 11031346 | Matching Sentences:
[ Sen. 13, subscore: 1.00 ]: RESULTS : Sera from 19 ( 86% ) of the 22 patients recognized a 9-kd protein , thus confirming this as the maize major allergen . This protein had an isoelectric point of greater than 9 , a molecular mass of 9047 . 0 d , and no glycosylation . Determination of its N-terminal sequence showed that it was a lipid transfer protein ( LTP ) . By using immunoblotting-inhibition experiments , we demonstrated that the LTP cross-reacts completely with rice and peach LTPs but not with wheat or barley LTPs . N-terminal sequence of the 16-kd allergen ( recognized by 36% of patients ) showed it to be the maize inhibitor of trypsin . This protein cross-reacts completely with grass , wheat , barley , and rice trypsin inhibitors . CONCLUSION : The major allergen of maize is an LTP with a molecular weight of 9 kd that is highly homologous with the peach LTP , the major allergen of the Prunoideae subfamily .
[ Sen. 14, subscore: 1.00 ]: This protein had an isoelectric point of greater than 9 , a molecular mass of 9047 . 0 d , and no glycosylation . Determination of its N-terminal sequence showed that it was a lipid transfer protein ( LTP ) . By using immunoblotting-inhibition experiments , we demonstrated that the LTP cross-reacts completely with rice and peach LTPs but not with wheat or barley LTPs . N-terminal sequence of the 16-kd allergen ( recognized by 36% of patients ) showed it to be the maize inhibitor of trypsin . This protein cross-reacts completely with grass , wheat , barley , and rice trypsin inhibitors . CONCLUSION : The major allergen of maize is an LTP with a molecular weight of 9 kd that is highly homologous with the peach LTP , the major allergen of the Prunoideae subfamily .
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| Title: Identification and characterization of the major allergens of buckwheat .
| | Author: Park JW Kang DB Kim CW koh SH Yum HY Kim KE Hong CS Lee KY .
| | Journal: Allergy Citation: V : 55 ( 11 ) P : 1035-41 Year: 2000 Type: ARTICLE | | Literature: oryza Field: abstract Doc ID: pub11097313 Accession (PMID): 11097313 | Matching Sentences:
[ Sen. 11, subscore: 1.00 ]: RESULTS : From the BW-allergic patients and asymptomatic controls , the sensitivity ( 100% ) , specificity ( 53% ) , and negative ( 100% ) and positive predictive values ( 73% ) of Pharmacia CAP specific IgE for diagnosis were estimated . The prevalence of IgE binding to 24-kDa ( pI 8 . 3 ) , 16-kDa ( pI 5 . 6 ) , and 9-kDa ( pI 5 . 0/ 6 . 0 ) allergens was higher than 50% in BW-allergic and asymptomatic subjects . However , the specific IgE to split 19-kDa ( pI 6 . 5/7 . 0 ) allergens were more specifically found in BW-allergic patients than in asymptomatic subjects ( 78% vs 7% ) . N-terminal amino-acid sequences of 19-kDa and 16-kDa allergens showed moderate and weak homology to the 19-kDa globulin protein of rice and alpha-amylase/trypsin inhibitor of millet , respectively . The N-terminus of the 9-kDa isoallergens were not different from each other and were identified as the reported trypsin inhibitors of BW . Attenuation of the IgE binding to the 9-kDa allergen was found with periodate oxidation . CONCLUSIONS : The allergens of 24 , 19 , 16 , and 9 kDa are strong candidates to be major allergens , and the 19-kDa allergen was relatively specific for BW-allergic patients . Moreover , measurement of BW-specific IgE and the features of immunoblotting should be very useful tools in the diagnosis of BW allergy .
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Score: 2.00 |
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| Title: Chloroplast fructose-1 , 6-bisphosphatase from Oryza differs in salt tolerance property from the Porteresia enzyme and is protected by osmolytes .
| | Author: Ghosh S Bagchi S Lahiri Majumder A | | Journal: Citation: V : 160 ( 6 ) P : 1171-1181 Year: 2001 Type: ARTICLE | | Literature: oryza Field: abstract Doc ID: pub11337074 Accession (PMID): 11337074 | Matching Sentences:
[ Sen. 8, subscore: 1.00 ]: Furthermore , chloroplastic fructose 1 , 6-bisphosphatase purified from salt-sensitive ( O sativa cv . IR26 ) and from the wild halophytic rice Porteresia coarctata differed in their in vitro salt tolerance property although they exhibited otherwise identical biochemical and immunological properties . This decline in enzyme activity was not correlated with de novo synthesis of the chloroplastic fructose-1 , 6-bisphosphatase protein in the presence of salt . The inhibitory effect of increasing concentration of NaCl on in vitro enzymatic activity could be prevented by preincubation of the enzyme with a number of osmolytes with an effectiveness in the order polyol>sugars . Further , the intrinsic tryptophan fluorescence of the purified rice enzyme is altered in vitro with increasing NaCl concentration which could be prevented by preincubation with inositol . Purified chloroplastic fructose-1 . 6-bisphosphatase from P coarctata however , exhibits no such inhibition of enzyme activity in vitro or alteration in tryptophan fluorescence with increasing NaCl concentration .
[ Sen. 9, subscore: 1.00 ]: IR26 ) and from the wild halophytic rice Porteresia coarctata differed in their in vitro salt tolerance property although they exhibited otherwise identical biochemical and immunological properties . This decline in enzyme activity was not correlated with de novo synthesis of the chloroplastic fructose-1 , 6-bisphosphatase protein in the presence of salt . The inhibitory effect of increasing concentration of NaCl on in vitro enzymatic activity could be prevented by preincubation of the enzyme with a number of osmolytes with an effectiveness in the order polyol>sugars . Further , the intrinsic tryptophan fluorescence of the purified rice enzyme is altered in vitro with increasing NaCl concentration which could be prevented by preincubation with inositol . Purified chloroplastic fructose-1 . 6-bisphosphatase from P coarctata however , exhibits no such inhibition of enzyme activity in vitro or alteration in tryptophan fluorescence with increasing NaCl concentration .
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