Browsing by Author "Katz, Woolf"

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    Rabies virus soluble antigens : a biochemical and biophysical study of the major antigen of rabies virus.
    (1967) Katz, Woolf; Katz, Woolf; Mead, T H
    The purpose of these investigations was to isolate and purify the largest of several antigens demonstrable in rabies-infected suckling mouse brains. The biochemical and biophysical properties of the antigen were studied with a view to elucidating its contribution to the intracellular synthesis and the structure of the virus particles. Extracts of normal and infected suckling mouse brains were purified by precipitation at pH 4.5 and freed of the smaller antigens by centrifugation prior to digestion with RNAase, DNAase and trypsin. The large antigen was purified by enzyme treatment, preparative ultracentrifugation, exclusion chroma tography and gradient centrifugation and appeared as rings varying in diameter between 8 and 12 mμ when examined by electron microscopy. Methods for the chemical estimation of pentose, deoxypentose and nitrogen were modified to meet the requirements of this investigation, and these techniques were used to determine the composition of the purified antigen. The antigen is a ribonucleoprotein, and found to be resistant to RNAase, DNAase, trypsin and chymotrypsin. A purified solution of the antigen contained 7.3μg RNA/ml., 11.4μg protein/ml and probably a trace of DNA. The success of this programme has resulted in the accumulation of certain original information which has been used in clari£ying the nature and structure of the largest soluble antigen.
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    Tanned gelatin: some biophysical and biochemical properties of a new gel exclusion agent and its application to the chromatography of proteins and viruses
    (1970) Katz, Woolf
    The principal aim of this study was to develop a new bed material suitable for gel exclusion chromatography, which would embrace all the desirable characteristics of available materials used for this purpose and if possible improve on some of them. The two most important limitations of existing gel media concern their exclusion limits and rigidity. Agar and agarose have been found satisfactory for the separation of larger molecules including some viruses, but difficulties may arise at low gel concentrations due to the low mechanical strength of the granules. The dextran and polyacrylamide gels have in general a rigidity equal to that of agar and agarose, but cannot be prepared with such large pore sizes and are therefore limited to the separation of smaller molecules.