Metadata of CSIR Papers
View Archive Info| Field | Value | |
| Creator |
Agrawal, P
Kumar, S Das, HR |
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| Subject |
Biochemistry & Molecular Biology
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| Description |
Matrix assisted laser desorption/ionization-time-of-flight (MALDI-TOF) mass spectrometric (MS) analysis of purified Arachis hypogaea stem lectin (SL-I) and its tryptic digests suggested it to be an isoformic glucose/mannose binding lectin. Two-dimensional gel electrophoresis of SL-I indicated six isoforms (A1-A6), which were confirmed by Western blotting and MALDI-TOF MS analysis. Comparative analysis of peptide mass spectra of the isoforrns matched with A. hypogaea lectins with three different accession numbers (Q43376_ARAHY, Q43377_ARAHY, Q70DJ5_ARAHY). Tandem mass spectrometric (MS/MS) analysis of tryptic peptides revealed these to be isoformic variants with altered amino acid sequences. Among the peptides, the peptide T12 showed major variation. The (199)Val-Ser-Tyr-Asn(202) sequence in peptide T12 of A1 and A2 was replaced by (199)Leu-Ser-His-Glu(202) in A3 and A4 (T12') while in A5 and A6 this sequence was (199)Val-Ser-Tyr-Val(202) (T12 ''). Peptide T1 showed the presence of (10)Asn in the isoforms A1-A5 while in A6 this amino acid was replaced by (10)Lys (T1'). Overall amino acid sequence as identified by MS/MS showed a high degree of similarity between A1, A2 and among A3, A4, AS. Carbohydrate binding domain and adenine binding site seem to be conserved. (C) 2010 Elsevier B.V. All rights reserved.
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| Publisher |
ELSEVIER SCIENCE BVAMSTERDAMPO BOX 211, 1000 AE AMSTERDAM, NETHERLANDS
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| Date |
2011-09-20T12:07:13Z
2011-09-20T12:07:13Z 2010 |
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| Type |
Article; Proceedings Paper
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| Identifier |
JOURNAL OF PROTEOMICS
1874-3919 http://hdl.handle.net/123456789/13157 |
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| Language |
English
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