Molecular cloning and characterization of a cDNA encoding α-glucosidase from spinach

Molecular cloning and characterization of a cDNA encoding α-glucosidase from spinach A cDNA encoding spinach α-glucosidase was cloned and sequenced bythe reverse-transcription polymerase chain reaction (RT-PCR) and rapidamplification of cDNA ends (RACE) methods. The cDNA comprised 2867 bp,and included an open reading frame which encodes a polypeptide of 903amino acid residues. The calculated molecular mass of 101 kDa waslarger than those of native α-glucosidases in spinach seeds,which are 78, 78, 82, and 82 kDa by SDS-PAGE for α-glucosidase I,II, III, and IV, respectively. The deduced amino acid sequence includedthose of tryptic peptides from native enzymes. Southern blot analysissuggested that the α-glucosidase gene was a single-copy gene.These results indicate the possibility that the multiplicity ofα-glucosidase in spinach occurs via post-translationalmodification. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Plant Molecular Biology Springer Journals

Molecular cloning and characterization of a cDNA encoding α-glucosidase from spinach

Loading next page...
 
/lp/springer_journal/molecular-cloning-and-characterization-of-a-cdna-encoding-glucosidase-f0FxOscpts
Publisher
Kluwer Academic Publishers
Copyright
Copyright © 1997 by Kluwer Academic Publishers
Subject
Life Sciences; Biochemistry, general; Plant Sciences; Plant Pathology
ISSN
0167-4412
eISSN
1573-5028
D.O.I.
10.1023/A:1005766003923
Publisher site
See Article on Publisher Site

Abstract

A cDNA encoding spinach α-glucosidase was cloned and sequenced bythe reverse-transcription polymerase chain reaction (RT-PCR) and rapidamplification of cDNA ends (RACE) methods. The cDNA comprised 2867 bp,and included an open reading frame which encodes a polypeptide of 903amino acid residues. The calculated molecular mass of 101 kDa waslarger than those of native α-glucosidases in spinach seeds,which are 78, 78, 82, and 82 kDa by SDS-PAGE for α-glucosidase I,II, III, and IV, respectively. The deduced amino acid sequence includedthose of tryptic peptides from native enzymes. Southern blot analysissuggested that the α-glucosidase gene was a single-copy gene.These results indicate the possibility that the multiplicity ofα-glucosidase in spinach occurs via post-translationalmodification.

Journal

Plant Molecular BiologySpringer Journals

Published: Sep 29, 2004

References

You’re reading a free preview. Subscribe to read the entire article.


DeepDyve is your
personal research library

It’s your single place to instantly
discover and read the research
that matters to you.

Enjoy affordable access to
over 12 million articles from more than
10,000 peer-reviewed journals.

All for just $49/month

Explore the DeepDyve Library

Unlimited reading

Read as many articles as you need. Full articles with original layout, charts and figures. Read online, from anywhere.

Stay up to date

Keep up with your field with Personalized Recommendations and Follow Journals to get automatic updates.

Organize your research

It’s easy to organize your research with our built-in tools.

Your journals are on DeepDyve

Read from thousands of the leading scholarly journals from SpringerNature, Elsevier, Wiley-Blackwell, Oxford University Press and more.

All the latest content is available, no embargo periods.

See the journals in your area

DeepDyve Freelancer

DeepDyve Pro

Price
FREE
$49/month

$360/year
Save searches from
Google Scholar,
PubMed
Create lists to
organize your research
Export lists, citations
Read DeepDyve articles
Abstract access only
Unlimited access to over
18 million full-text articles
Print
20 pages/month
PDF Discount
20% off