Zobrazeno 1 - 10
of 28
pro vyhledávání: '"Wijaya Altekar"'
Publikováno v:
World Journal of Microbiology and Biotechnology. 13:561-564
Fructose-1,6-bisphosphate (FBP) aldolase (EC 4.1.2.13) of Haloferax mediterranei was immobilized by treating the cell extract in the presence of 10% BSA, with the cross-linking reagent, 0.5% glutaraldehyde for 15min, with the retention of 60% of its
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::7558aa5d4f8fccc6e3ad3645ac20c592
https://doi.org/10.1023/a:1018521510665
https://doi.org/10.1023/a:1018521510665
Publikováno v:
Journal of Biochemical and Biophysical Methods. 24:239-247
The cells of Haloferax mediterannei were stabilized by cross-linking with 0.5% glutaraldehyde for 10 min. Such cells were found to be osmotically stable even when suspended in water. The stabilized cells could be permeabilized by treatment with chlor
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::87d6f22a80beb9318f9b9ed3d35562c2
https://doi.org/10.1016/0165-022x(94)90076-0
https://doi.org/10.1016/0165-022x(94)90076-0
Autor:
Vidhya Rangaswamy, Wijaya Altekar
Publikováno v:
FEMS Microbiology Letters. 83:241-246
Ketohexokinase, catalysing the ATP-dependent phosphorylation of D -fructose to fructose 1-phosphate was identified as the enzyme responsible for the initiation of fructose breakdown via the modified EMP pathway in the halophilic arachaebacterium Halo
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::81a570109f90e93e3270ccd46936c57b
https://doi.org/10.1111/j.1574-6968.1991.tb04471.x
https://doi.org/10.1111/j.1574-6968.1991.tb04471.x
Autor:
Gomathi Krishnan, Wijaya Altekar
Publikováno v:
European Journal of Biochemistry. 195:343-350
An electrophoretically homogeneous class I (Schiff base) alsolase has been isolated for the first time from the archaebacterial halophile Haloarcula (Halobacterium) vallismortis. The aldolase was characterized with respect to its molecular mass, amin
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0a9f3f1e56d0498490b8350ca4d821d4
https://doi.org/10.1111/j.1432-1033.1991.tb15712.x
https://doi.org/10.1111/j.1432-1033.1991.tb15712.x
Autor:
Vidhya Rangaswamy, Wijaya Altekar
Publikováno v:
FEMS Microbiology Letters. 69:139-143
The breakdown of fructose in Haloarcula (Halobacterium) vallismortis probably takes place via a novel modification of Embden Meyerhof-Parnas (EMP) pathway. Phosphorylation of fructose to yield frutose 1-phosphate as the product appears to be the init
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::c195a7017733da3fea9b16b8f9ed4bc1
https://doi.org/10.1111/j.1574-6968.1990.tb04190.x
https://doi.org/10.1111/j.1574-6968.1990.tb04190.x
Autor:
Wijaya Altekar, Gomathi Krishnan
Publikováno v:
The Journal of General and Applied Microbiology. 36:19-32
Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) was purified to electrophoretic homogeneity from the halophilic archaebacterium Haloarcula (Halobacterium) vallismortis. The purification was achieved by (NH4)2SO4-mediated chromatography on Sepharose
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::f67b3305a5829be1e84a5b8bd9506b73
https://doi.org/10.2323/jgam.36.19
https://doi.org/10.2323/jgam.36.19
Autor:
Rema Rajagopalan, Wijaya Altekar
Publikováno v:
Archives of Microbiology. 153:169-174
Among the several strains of halobacteria grown heterotrophically, ribulose bisphosphate carboxylase activity was detected in those which accumulate poly (β-hydroxybutyrate), viz. Haloferax mediterranei, Haloferax volcanii and Halobacterium marismor
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::ccae8fd4ca597d6be97fc4fae0900714
https://doi.org/10.1007/bf00247816
https://doi.org/10.1007/bf00247816
Autor:
Wijaya Altekar, Sandra E. D'Souza
Publikováno v:
The Journal of general and applied microbiology. 44(4)
Fructose-1,6-bisphosphate (FBP) aldolase (EC 4.1.2.13) was purified 97-fold from a halophilic archaebacterium Haloferax mediterranei, with a specific activity of 2.8. The enzyme was characterized as a Class II aldolase on the basis of its inhibition
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::381a69fbfa092ceb075c8acad646ed51
https://pubmed.ncbi.nlm.nih.gov/12501417
https://pubmed.ncbi.nlm.nih.gov/12501417
Small-angle neutron scattering study of halophilic glyceraldehyde 3-phosphate dehydrogenase (hGAPDH)
Publikováno v:
Physica B: Condensed Matter. 174:306-308
hGAPDH has a radius of gyration of 32±0.5 A in high salt concentration, and a shape similar to an oblate ellipsoid of axial ratio 0.5 but with a much larger specific surface. The enzyme dissociates and unfolds in low salt solutions. These results ar
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::ff8be2d0686dfae8044883e5d36e1d21
https://doi.org/10.1016/0921-4526(91)90622-l
https://doi.org/10.1016/0921-4526(91)90622-l
Adaptive response of Haloferax mediterranei to low concentrations of NaCl (20%) in the growth medium
Publikováno v:
Archives of microbiology. 168(1)
Halobacteria require 20-25% NaCl for optimal growth and lyse when the salt concentration falls below 10%. The response of Haloferax mediterranei cells to low concentrations of NaCl (< 20%) in the medium was studied. The cells adapted to and grew in c
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b161924545f2535b85133146aabcadc3
https://pubmed.ncbi.nlm.nih.gov/9211716
https://pubmed.ncbi.nlm.nih.gov/9211716