Alcohol oxidase of methylotrophic thermo- and acidotolerant yeast Hansenula sp
Jazyk angličtina Země Spojené státy americké Médium print
Typ dokumentu časopisecké články
PubMed
2680833
DOI
10.1007/bf02821297
Knihovny.cz E-zdroje
- MeSH
- alkoholoxidoreduktasy izolace a purifikace metabolismus MeSH
- elektroforéza v polyakrylamidovém gelu MeSH
- kinetika MeSH
- koncentrace vodíkových iontů MeSH
- makromolekulární látky MeSH
- Pichia enzymologie MeSH
- Saccharomycetales enzymologie MeSH
- vysokoúčinná kapalinová chromatografie MeSH
- Publikační typ
- časopisecké články MeSH
- Názvy látek
- alkoholoxidoreduktasy MeSH
- makromolekulární látky MeSH
Electrophoretic analysis of alcohol oxidase purified from the methylotrophic thermo- and acidotolerant yeast Hansenula sp. revealed the presence of two active forms of the enzyme with molar mass 440 kg/mol (major component) and 724 kg/mol (minor component). A subunit M of the enzyme was found to be 72 kg/mol. Two active forms of the enzyme found by electrophoresis seem to be caused by dissociation of the octameric form to the tetramer under alkaline conditions. Studies of alcohol oxidase showed a kinetic variability of the enzyme with respect to its Km. It is proposed that the variability of Km is caused by enzyme binding to formaldehyde.
