PubMed HealthSearch

Biomedical subjects

J A Hewitt

Publications and source records attributed to J A Hewitt.

9 recordsLinked to original sources

Controlled proteolytic digestion of the M-protein of Sendai virus: the isolation of a fragment of 30000 molecular weight.

Proteolytic digestion of the M-protein of Sendai virus produces a product with a mol. wt. approximately 5000 less than that of the intact protein. In the case of digestion with chymotrypsin this cleavage is quite specific and the cleaved protein can be isolated. The smaller fragment appears to be physically removed from the larger (30000 mol. wt.) fragment, rather than remaining in non-covalent association with it. The cleavage is likely to be near the N-terminus of the protein. At the present time there is no indication of the biological function of this fragment.

Amino Acids

A morphological study of the M-protein of Sendai virus.

A purification scheme is described for the M-protein of Sendai virus and an electron microscope study of the isolated protein is presented. The protein exists as subunits of 6 nm in diam., which possess a central hole; the subunits may be dimers of the polypeptide. They are able to form filamentous aggregates which wind around one another to form a helical structure. It is suggested that these filaments may be the form adopted by the protein in the virus, the filaments lying parallel to one another just beneath the virus membrane to form a shell, but that the helical form is likely to be a property only of the isolated protein.

Microscopy, Electron

Miniphage-a class of satellite phage to M13.

Satellite or defective bacteriophage particles can appear in extensively recycled stocks of coliphage M13. These particles, herein known as miniphage, replicate using the wild type bacteriophage as a helper. Their physical properties (u.v. spectra, sedimentation of DNA and bacterophage, electrophoretic moblitiy) are described and a method for the isolation of specific satellite bacteriophage is presented.

Amino Acids