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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | Vorob'ev, M. M. Rao, N. M. Kochetkov, K. A. |
| Description | Country affiliation: RUSSIA Author Affiliation: Vorob'ev MM ( A.N. Nesmeyanov Institute of Organoelement Compounds, Russian Academy of Sciences, Moscow, Russia. mmvor@ineos.ac.ru.); Rao NM ( Centre for Cell and Molecular Biology, Hyderabad, India.); Kochetkov KA ( A.N. Nesmeyanov Institute of Organoelement Compounds, Russian Academy of Sciences, Moscow, Russia.) |
| Abstract | Proteolysis of ß-lactoglobulin by trypsin was studied with fluorescence spectroscopy and an empirical exponential model was engaged to describe the peptide bond hydrolysis kinetics. The shift in the fluorescence maximum of tryptophan residues, from 342 to 352 nm, in the course of ß-lactoglobulin degradation was used as an indicator of the transition of masked peptide bonds to the demasked ones, which were accessible for the enzyme action. A simple equation with only two parameters was suggested to link together the degree of demasking of peptide bonds and the degree of their hydrolysis, allowing the kinetic description of proteolysis. |
| File Format | HTM / HTML |
| ISSN | 16076729 |
| Issue Number | 1 |
| Volume Number | 471 |
| e-ISSN | 16083091 |
| Journal | Doklady Biochemistry and Biophysics |
| Language | English |
| Publisher | Springer |
| Publisher Date | 2016-11-01 |
| Publisher Place | Russian Federation |
| Access Restriction | One Nation One Subscription (ONOS) |
| Subject Keyword | Discipline Biophysics Discipline Biochemistry Lactoglobulins Chemistry Models, Chemical Trypsin Algorithms Caseins Hydrolysis Kinetics Proteolysis Spectrometry, Fluorescence Time Factors Tryptophan Journal Article |
| Content Type | Text |
| Resource Type | Article |
| Subject | Chemistry Medicine Biochemistry Biophysics |
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