GONUTS has been updated to MW1.31 Most things seem to be working but be sure to report problems.
PMID:37167
| Citation |
Carroll, SF and Martinez, RJ (1979) Purification and properties of rabbit alveolar macrophage lysozyme. Infect. Immun. 24:460-7 |
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| Abstract |
Lysozyme was isolated from Bacillus Calmette-Guerin-elicited rabbit alveolar macrophages by acid extraction and purified to homogeneity by a single-column procedure. Yields of the purified enzyme averaged between 20 and 30 mg per rabbit, values far in excess of those obtained with previously published methods. Rabbit lysozyme has a molecular weight of 14,300 and exhibits optimal lytic activity against Micrococcus lysodeikticus at an ionic strength of 0.04, pH 6.5. Our results indicate that lysozyme and other granule components can be fractionated from elicited alveolar macrophages by using simple techniques, suggesting methods for the bulk purification of lysosomal constituents. |
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| Keywords |
Amino Acids/analysis; Animals; Chromatography; Hydrogen-Ion Concentration; Macrophages/enzymology; Micrococcus/metabolism; Muramidase/analysis; Muramidase/isolation & purification; Osmolar Concentration; Pulmonary Alveoli/cytology; Rabbits |
Significance
Annotations
| Gene product | Qualifier | GO Term | Evidence Code | with/from | Aspect | Extension | Notes | Status |
|---|---|---|---|---|---|---|---|---|
| GO:0003796: lysozyme activity |
ECO:0000314: |
F |
Figure 5 shows the relative activity between the initial rate of lysis and the concentration of lysozyme in the hen egg white, which represent a linear relationship. Since the slope of the graph is positive, it shows that as the concentration of lysozyme C increases, the rate of lysis will also increase. |
complete | ||||
| GO:0003796: lysozyme activity |
ECO:0000314: |
F |
Figure 5 shows the positive linear relationship between the initial rate of lysis of a cell suspension and lysozyme concentration under optimal conditions for rabbit lysozyme. Since the slope is positive, it shows that as the concentration of lysozyme C increases, the rate of lysis also increases. After adding together the total number of calculated amino acid residues found in Table 2, you find that it is 129.4 which is closest to the 130 in the lysozyme C as found on uniprot. |
complete | ||||
Notes
See also
References
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