Abstract:
:The kinetic properties of collagen-bound firefly luciferase have been investigated. Under definite hydrodynamic conditions with low agitation in the reaction medium, the observed behavior is modified compared to the enzyme free in solution: reducing the stirring rate decreases the observed enzymatic activity. But diffusional resistances alone cannot account for these atypical kinetics though mass transfer may certainly play an important role during the transient state of the bioluminescent reaction. After immobilization, the time necessary to reach the steady state increased from 300 ms to 3 min and the two substrates, luciferin and ATP, behave differently with respect to the enzyme: The nature of the saturating substrate first in contact with the bound enzyme is not indifferent suggesting that immobilization can reveal behaviors or mechanisms which are not visualized with the free enzyme.
journal_name
Biotechnol Bioengjournal_title
Biotechnology and bioengineeringauthors
Blum LJ,Coulet PRdoi
10.1002/bit.260280804subject
Has Abstractpub_date
1986-08-01 00:00:00pages
1154-8issue
8eissn
0006-3592issn
1097-0290journal_volume
28pub_type
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journal_title:Biotechnology and bioengineering
pub_type: 杂志文章
doi:10.1002/bit.260420409
更新日期:1993-08-05 00:00:00
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journal_title:Biotechnology and bioengineering
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journal_title:Biotechnology and bioengineering
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journal_title:Biotechnology and bioengineering
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journal_title:Biotechnology and bioengineering
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journal_title:Biotechnology and bioengineering
pub_type: 杂志文章
doi:10.1002/bit.260401018
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journal_title:Biotechnology and bioengineering
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更新日期:1983-01-01 00:00:00
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doi:10.1002/bit.260341105
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journal_title:Biotechnology and bioengineering
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journal_title:Biotechnology and bioengineering
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journal_title:Biotechnology and bioengineering
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doi:
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