- Library Home /
- Search Collections /
- Open Collections /
- Browse Collections /
- UBC Theses and Dissertations /
- Studies in the 'Lioxidase' in the flesh of British...
Open Collections
UBC Theses and Dissertations
UBC Theses and Dissertations
Studies in the 'Lioxidase' in the flesh of British Columbia herring Khan, Muhammed Mujibur Rahman
Abstract
From the dark muscle of British Columbia herring a highly active enzyme capable of peroxidising unconjugated unsaturated fatty acids was isolated. This ‘lipoxidase’, which was shown to be a nitrogenous complex possessing no heavy metals or sulphydryl group as the active centre, is heat-labile and can act only in presence of activators such as certain iron-containing organic nitrogenous compounds. Two such compounds, namely haemoglobin and cytochrome ‘C’ were isolated. The enzyme exhibits optimum activity at 15°C. and pH 6.9. There is also an optimum concentration of enzyme, substrate, and of the activators for maximum enzyme activity. The presence of the activators appears to change the kinetics of the reactions. The inhibition of the enzymic reaction brought about by cyanide and azide is possibly due to the inactivation of the iron-containing activators rather than of the enzyme itself.
Item Metadata
Title |
Studies in the 'Lioxidase' in the flesh of British Columbia herring
|
Creator | |
Publisher |
University of British Columbia
|
Date Issued |
1950
|
Description |
From the dark muscle of British Columbia herring a highly active enzyme capable of peroxidising unconjugated unsaturated fatty acids was isolated. This ‘lipoxidase’, which was shown to be a nitrogenous complex possessing no heavy metals or sulphydryl group as the active centre, is heat-labile and can act only in presence of activators such as certain iron-containing organic nitrogenous compounds. Two such compounds, namely haemoglobin and cytochrome ‘C’ were isolated. The enzyme exhibits optimum activity at 15°C. and pH 6.9. There is also an optimum concentration of enzyme, substrate, and of the activators for maximum enzyme activity. The presence of the activators appears to change the kinetics of the reactions. The inhibition of the enzymic reaction brought about by cyanide and azide is possibly due to the inactivation of the iron-containing activators rather than of the enzyme itself.
|
Genre | |
Type | |
Language |
eng
|
Date Available |
2012-03-06
|
Provider |
Vancouver : University of British Columbia Library
|
Rights |
For non-commercial purposes only, such as research, private study and education. Additional conditions apply, see Terms of Use https://open.library.ubc.ca/terms_of_use.
|
DOI |
10.14288/1.0302628
|
URI | |
Degree | |
Program | |
Affiliation | |
Degree Grantor |
University of British Columbia
|
Campus | |
Scholarly Level |
Graduate
|
Aggregated Source Repository |
DSpace
|
Item Media
Item Citations and Data
Rights
For non-commercial purposes only, such as research, private study and education. Additional conditions apply, see Terms of Use https://open.library.ubc.ca/terms_of_use.