| 17 matches found in 13 documents. Search time: 0.141 seconds. |
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| Title: Rice alpha-mannosidase digesting the high mannose glycopeptide of glutelin .
| | Author: Kishimoto T Hori H Takano D Nakano Y Watanabe M Mitsui T | | Journal: Citation: V : 112 ( 1 ) P : 15-24 Year: 2001 Type: ARTICLE | | Literature: oryza Field: abstract Doc ID: pub11319010 Accession (PMID): 11319010 | | Abstract: alpha-Mannosidase ( EC 3 . 2 . 1 . 24 ) from rice dry seeds was purified to homogeneity .
Optimum pH and Km for pNP-alpha-Man hydrolysis were pH 4 . 3-4 . 5 and 1 . 04 mM , respectively .
The enzyme digested mannobioses such as Manalpha-1 , 2Man , Manalpha-1 , 6Man , Manalpha-1 , 3Man but Manalpha-1 , 4Man .
Zn2+ ion was required for the activity , whereas EDTA and swainsonine inhibited the activity by 80 and 96% , respectively .
The rice storage protein , glutelin was prepared and its basic subunits were shown to have high mannose-type sugar chains by two-dimensional mapping using NH2-P and C18 silica columns .
They were Man9GlcNAc2 , Man8GlcNAc2 , Man7GlcNAc2 , Man6GlcNAc2 and Man5GlcNAc2 .
All these oligosaccharides were digested by the purified alpha-mannosidase , and Man-GlcNAc2 and mannose were formed .
Glycopeptides , having these high mannose-type sugar chains , could also be digested by the alpha-mannosidase .
Subunits were prepared from glutelin basic subunit and the richest subunit among them , subunit 2 ( isoform 2 ) , was digested by the alpha-mannosidase .
Isoform 2 was digested by V8 protease only partially and slowly .
However , isoform 2 , pre-treated with the alpha-mannosidase , was rapidly and completely digested by V8 protease .
| Matching Sentences:
[ Sen. 10, subscore: 1.00 ]: Isoform 2 was digested by V8 protease only partially and slowly .
[ Sen. 11, subscore: 1.00 ]: However , isoform 2 , pre-treated with the alpha-mannosidase , was rapidly and completely digested by V8 protease .
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| Title: Comparison of the structure of the extrinsic 33 kDa protein from different organisms .
| | Author: Tohri A Suzuki T Okuyama S Kamino K Motoki A Hirano M Ohta H Shen JR Yamamoto Y Enami I | | Journal: Plant Cell Physiol .
Citation: V : 43 ( 4 ) P : 429-39 Year: 2002 Type: ARTICLE | | Literature: oryza Field: abstract Doc ID: pub11978871 Accession (PMID): 11978871 | | Abstract: The psbO gene encoding the extrinsic 33 kDa protein of oxygen-evolving photosystem II ( PSII ) complex was cloned and sequenced from a red alga , Cyanidium caldarium .
The gene encodes a polypeptide of 333 residues , of which the first 76 residues served as transit peptides for transfer across the chloroplast envelope and thylakoid membrane .
The mature protein consists of 257 amino acids with a calculated molecular mass of 28 , 290 Da .
The sequence homology of the mature 33 kDa protein was 42 . 9-50 . 8% between the red alga and cyanobacteria , and 44 . 7-48 . 6% between the red alga and higher plants .
The cloned gene was expressed in Escherichia coli , and the recombinant protein was purified , subjected to protease-treatments .
The cleavage sites of the 33 kDa protein by chymotrypsin or V8 protease were determined and compared among a cyanobacterium ( Synechococcus elongatus ) , a euglena ( Euglena gracilis ) , a green alga ( Chlamydomonas reinhardtii ) and two higher plants ( Spinacia oleracea and Oryza sativa ) .
The cleavage sites by chymotrypsin were at 156F and 190F for the cyanobacterium , 159M , 160F and 192L for red alga , 11Y and 151F for euglena , 10Yand 150F for green alga , and 16Y for spinach , respectively .
The cleavage sites by V8 protease were at 181E ( cyanobacterium ) , 182E and 195E ( red alga ) , 13E , 67E , 69E , 153D and 181E ( euglena ) , 176E and 180E ( green alga ) , and 18E or 19E ( higher plants ) .
Since most of the residues at these cleavage sites were conserved among the six organisms , the results indicate that the structure of the 33 kDa protein , at least the structure based on the accessibility by proteases , is different among these organisms .
In terms of the cleavage sites , the structure of the 33 kDa protein can be divided into three major groups : cyanobacterial and red algal-type has cleavage sites at residues around 156-195 , higher plant-type at residues 16-19 , and euglena and green algal-type at residues of both cyanobacterial and higher plant-types . | Matching Sentences:
[ Sen. 6, subscore: 1.00 ]: The cleavage sites of the 33 kDa protein by chymotrypsin or V8 protease were determined and compared among a cyanobacterium ( Synechococcus elongatus ) , a euglena ( Euglena gracilis ) , a green alga ( Chlamydomonas reinhardtii ) and two higher plants ( Spinacia oleracea and Oryza sativa ) .
[ Sen. 8, subscore: 1.00 ]: The cleavage sites by V8 protease were at 181E ( cyanobacterium ) , 182E and 195E ( red alga ) , 13E , 67E , 69E , 153D and 181E ( euglena ) , 176E and 180E ( green alga ) , and 18E or 19E ( higher plants ) .
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Score: 2.00 |
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| Title: RNA-binding domain of the key structural protein P7 for the Rice dwarf virus particle assembly .
| | Author: Zhong BX Shen YW Omura T | | Journal: Acta Biochim . Biophys . Sin . ( Shanghai ) Citation: V : 37 ( 1 ) P : 55-60 Year: 2005 Type: ARTICLE | | Literature: oryza Field: abstract Doc ID: pub15645082 Accession (PMID): 15645082 | | Abstract: The Rice dwarf virus ( RDV ) P7 structural protein is the key protein in the RDV particle assembly .
The P7 protein was digested partially or completely by Staphylococcus aureus V8 protease and/or Pseudomonas fragi Asp-N protease .
The molecular mass and the N-terminal amino acid sequence of the polypeptide fragments of the P7 protein were determined by SDS-PAGE and the Edman degradation method , respectively .
Then the polypeptides were located in the deduced amino acid sequence of the RDV P7 protein based on the nucleotide sequence information , with the knowledge of the specific cleavage sites of the Staphylococcus aureus V8 and Pseudomonas fragi Asp-N protease , and the two RNA-binding domains in the P7 protein were identified .
Domain 1 was located in the residue 128-249 containing 122 amino acids and domain 2 was located in the residue 325-355 containing 31 amino acids .
Thus , these two domains may play an important role in the virus particle assembly by contributing to the packaging of viral dsRNAs inside the particles .
The two domains may be novel RNA-binding domains , because no amino acid sequences highly similar to the conservative sequences of known dsRNA-binding domains reported so far .
The similarity between the motif of domain 1 and the motif of the DNA-binding protein suggests that the DNA-binding activity of the RDV P7 protein may be due to this sequence .
The similarity between the motif of domain 1 and the motif of the RNA polymerase domain suggests that the P7 protein may also play a role in RNA synthesis , besides its function in the assembly and subsequent packaging of viral dsRNA into core particles .
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[ Sen. 2, subscore: 1.00 ]: The P7 protein was digested partially or completely by Staphylococcus aureus V8 protease and/or Pseudomonas fragi Asp-N protease .
[ Sen. 4, subscore: 1.00 ]: Then the polypeptides were located in the deduced amino acid sequence of the RDV P7 protein based on the nucleotide sequence information , with the knowledge of the specific cleavage sites of the Staphylococcus aureus V8 and Pseudomonas fragi Asp-N protease , and the two RNA-binding domains in the P7 protein were identified .
| | Supplemental links/files: reference in endnote online text related articles pubmed citation | |
Score: 2.00 |
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| Title: Outer capsid protein heterogeneity of rice dwarf phytoreovirus .
| | Author: Suzuki N Sugawara M | | Journal: J Gen . Virol . Citation: V : 72 ( Pt 9 ) ( ) P : 2239-42 Year: 1991 Type: ARTICLE | | Literature: oryza Field: abstract Doc ID: pub1895060 Accession (PMID): 1895060 | | Abstract: The 46K outer capsid protein encoded by RNA segment S8 and the 42K polypeptide , previously thought to be the segment S9-encoded structural protein , were isolated from a rice dwarf phytoreovirus purified preparation , and then analysed by peptide mapping and electroblot-ELISA .
Staphylococcus aureus V8 protease peptide mapping patterns of the 42K and 46K proteins were similar .
Two monoclonal antibodies ( MAbs ) , obtained after immunization with virus particles dissociated by 0 . 1% SDS , were each specific for both the 42K and 46K proteins .
Furthermore , the MAbs bound common peptide fragments which were generated by digestion of the 42K and 46K proteins with V8 protease or proteinase K These results strongly suggest that the 42K protein is not a gene product of S9 but a product overlapping with the 46K outer capsid protein .
Whether the two proteins are functionally distinct remains to be determined . | Matching Sentences:
[ Sen. 2, subscore: 1.00 ]: Staphylococcus aureus V8 protease peptide mapping patterns of the 42K and 46K proteins were similar .
[ Sen. 4, subscore: 1.00 ]: Furthermore , the MAbs bound common peptide fragments which were generated by digestion of the 42K and 46K proteins with V8 protease or proteinase K These results strongly suggest that the 42K protein is not a gene product of S9 but a product overlapping with the 46K outer capsid protein .
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Score: 1.00 |
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| Title: The amino acid sequence of a 20 kDa bifunctional subtilisin/alpha-amylase inhibitor from bran [ correction of brain ] of rice ( Oryza sativa L ) seeds .
| | Author: Ohtsubo K Richardson M | | Journal: FEBS Lett .
Citation: V : 309 ( 1 ) P : 68-72 Year: 1992 Type: ARTICLE | | Literature: oryza Field: abstract Doc ID: pub1511747 Accession (PMID): 1511747 | | Abstract: A 20 kDa bifunctional inhibitor of the microbial proteinase , subtilisin , and the alpha-amylase from the larvae of the red flour beetle ( Tribolium castaneum ) was purified from bran of rice seeds by saline extraction , precipitation with ammonium sulphate , ion-exchange chromatography on DEAE-Cellulose and Toyopearl CM-650 , and preparative HPLC on Vydac C18 .
The complete primary structure was determined by automatic degradation of the intact , reduced and S-alkylated protein , and by manual DABITC/PITC micro-sequencing of peptides obtained from the protein following separate enzymic digestions with trypsin , pepsin , chymotrypsin , elastase and the protease from S aureus V8 .
The protein sequence , which contained 176 residues , showed strong homology with similar bifunctional inhibitors previously isolated from wheat and barley which are related to the Kunitz family of proteinase inhibitors from legume seeds . | Matching Sentences:
[ Sen. 2, subscore: 1.00 ]: The complete primary structure was determined by automatic degradation of the intact , reduced and S-alkylated protein , and by manual DABITC/PITC micro-sequencing of peptides obtained from the protein following separate enzymic digestions with trypsin , pepsin , chymotrypsin , elastase and the protease from S aureus V8 .
| | Supplemental links/files: reference in endnote online text related articles pubmed citation | |
