1994 Fiscal Year Final Research Report Summary
Molecular Cloning of Cation Transporting ATPases from Plasmodium falciparum.
| Project/Area Number |
05670236
|
|---|
| Research Category |
Grant-in-Aid for General Scientific Research (C)
|
| Allocation Type | Single-year Grants |
|---|
| Research Field |
寄生虫学(含医用動物学)
|
|---|
| Research Institution | OSAKA CITY UNIVERSITY |
|---|
Principal Investigator |
KIMURA Masatsugu Osaka City Univ.Med.Sch.Research Assistant, 医学部, 助手 (60195378)
|
|---|
| Co-Investigator(Kenkyū-buntansha) |
TANABE Kazuyuki Osaka College of Technology Professor, 教授 (40047410)
|
|---|
| Project Period (FY) |
1993 – 1994
|
| Keywords | P-type ATPase / Cloning / Plasmodium / yoelii / expression |
|---|
| Research Abstract |
AP type ATPase gene was cloned from the genomic libraries of Plasmodium yoelii.Sequencing of partial cDNA clones of the gene identified an intron near the 3'-end of the gene.The deduced amino acid sequence predicted a 220 kDa protein with a total of 1877 amino acids.The amino acid sequence shares homology with a family of P-type cation transporting ATPases in conserved regions important for phosphorylation, ATP-binding, or conformational change.It had the highest amino acid sequence homology (26.7%/851 aa) to the P.falciparum ATP1 which was considered as alpha-subunit of Na^+/K^+-ATPase.
The P.yoelii ATPase (PyATP1) seemed to have a hydrophillic extra amino acid sequence in a region between the phosphorylation site and the fluorescein isothiocyanate-binding site of P-type ATPases.Such an extra hydrophillic region was seen in other malarial ATPases.The region was expressed in E.coli and polyclonal antibodies were made by using the expressed peptide and also an oligopeptide of pentapeptide repeats found in the region.A 195-200 kDa band was reacted commonly with these antibodies in Western blotting.PyATP1 seemed to be an organellar ATPase from indirect immunofluorescence assay.
|
Research Products
(12 results)
