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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
2
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pubmed:dateCreated |
1994-4-11
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pubmed:abstractText |
The complete amino acid sequence of rye seed chitinase-a (RSC-a) has been analyzed. RSC-a was cleaved with cyanogen bromide and the resulting three fragments, CB1, CB2, and CB3, were separated by gel filtration. The amino acids of the N-terminal fragment CB1 were sequenced by analyzing the peptides produced by digestion with trypsin, lysylendopeptidase, or pepsin of reduced S-carboxymethylated or S-aminoethylated CB1. The sequences of fragments CB2 and CB3 were established by sequencing the tryptic peptides from reduced S-carboxymethylated CB2 and CB3, and by aligning them with the sequence of rye seed chitinase-c (RSC-c) to maximize sequence homology. The complete amino acid sequence of RSC-a was established by connecting these three fragments. RSC-a consists of 302 amino acid residues including hydroxyproline residues, and has a molecular mass of 31,722 Da. RSC-a is basic protein with a cysteine-rich amino terminal domain, indicating that this enzyme belongs to class I chitinases. The amino acid sequence of RSC-a showed that the sequence from Gly60 to C-terminal Ala302 in this enzyme corresponds to that of RSC-c belonging to class II chitinases with 92% identity, and that RSC-a has high similarity to other plant class I chitinases but a longer hinge region and an extra disulfide bond.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
B
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Chitinase,
http://linkedlifedata.com/resource/pubmed/chemical/Cyanogen Bromide,
http://linkedlifedata.com/resource/pubmed/chemical/Isoenzymes,
http://linkedlifedata.com/resource/pubmed/chemical/Peptides,
http://linkedlifedata.com/resource/pubmed/chemical/Plant Proteins
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pubmed:status |
MEDLINE
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pubmed:month |
Feb
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pubmed:issn |
0916-8451
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
58
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
322-9
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:7764543-Amino Acid Sequence,
pubmed-meshheading:7764543-Chitinase,
pubmed-meshheading:7764543-Cyanogen Bromide,
pubmed-meshheading:7764543-Isoenzymes,
pubmed-meshheading:7764543-Molecular Sequence Data,
pubmed-meshheading:7764543-Peptides,
pubmed-meshheading:7764543-Plant Proteins,
pubmed-meshheading:7764543-Secale cereale,
pubmed-meshheading:7764543-Seeds,
pubmed-meshheading:7764543-Sequence Homology, Amino Acid
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pubmed:year |
1994
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pubmed:articleTitle |
The complete amino acid sequence of chitinase-a from the seeds of rye (Secale cereal).
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pubmed:affiliation |
Laboratory of Protein Chemistry & Engineering, Faculty of Agriculture, Kyushu University, Fukuoka, Japan.
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pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, Non-U.S. Gov't
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