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| Content Provider | Journal of Biological Chemistry (JBC) |
|---|---|
| Author | Cumsky, M. G. Zusman, D. R. |
| Abstract | Myxococcus xanthus is a Gram-negative bacterium that has a complex life cycle which includes cellular aggregation and sporulation. During the period of cellular aggregation, a lectin-like protein called myxobacterial hemagglutinin (MBHA) is synthesized. A four-step purification procedure for MBHA is described. It consists of chromatography on DEAE-cellulose, CM-cellulose, and hydroxyapatite, followed by gel filtration on Bio-Gel P-30. This procedure gives good yields of MBHA (40-50%) free of contaminating proteins. The purified protein has been partially characterized. It exists as a monomer in solution with an apparent Mr = 28,000 and an isoelectric point of 8.3. The amino acid composition of MBHA has been determined. It shows a very high content of glycine (19%) as well as aromatic amino acids (9%); it has a low percentage of charged amino acids. No detectable carbohydrate was found in a large sample (50 micrograms) of MBHA. The far-ultraviolet CD spectrum of MBHA indicates a secondary structure which contains very little alpha-helix, 50 +/- 10% beta-sheet, and 50 +/- 10% random coil. MBHA comprises 1-2% of soluble protein of M. xanthus at the time of cellular aggregation. The fact that it is a lectin suggests that it may play a role in cell-cell recognition or adhesion. |
| Related Links | http://www.jbc.org/content/256/23/12581.abstract |
| Ending Page | 12588 |
| Starting Page | 12581 |
| Page Count | 8 |
| File Format | HTM / HTML PDF |
| ISSN | 00219258 |
| Journal | Journal of Biological Chemistry (JBC) |
| Issue Number | 23 |
| Volume Number | 256 |
| e-ISSN | 1083351X |
| Language | English |
| Publisher | American Society for Biochemistry and Molecular Biology |
| Publisher Date | 1981-12-10 |
| Access Restriction | Open |
| Content Type | Text |
| Resource Type | Article |
| Subject | Cell Biology Biochemistry Molecular Biology |
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