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Biomedical subjects

J Mann

Publications and source records attributed to J Mann.

At least 397 records · Page 22Linked to original sources

Transfer of thymidine kinase to thymidine kinaseless L cells by infection with ultraviolet-irradiated herpes simplex virus.

L cells lacking thymidine kinase (TK) activity (Ltk(-) cells) have been stably transformed to a TK-positive phenotype by infection with ultraviolet-irradiated herpes simplex virus (HSV-UV). The highest frequency of the Ltk(-) to Ltk(+) transformation observed in these experiments was approximately 10(-3), whereas no measurable transformation was observed (less than 10(-8)) in the absence of HSV-UV infection. Cell lines of HSV-transformed Ltk(+) cell lines contain 7 to 24 times as much TK activity as do the parental Ltk(-) cells, and they have been maintained in culture for a period exceeding 8 months. The kinetics of thermal inactivation of the TK activity derived from an Ltk(+) HSV-transformed cell line and the TK activity from Ltk(-) cells lytically infected with infectious HSV are similar. Both of these TK activities are much more thermolabile than the TK activity present in wild-type L cells. A mutant strain of HSV which does not induce TK activity during lytic infection does not cause the Ltk(-) to Ltk(+) transformation. These data suggest that either an HSV TK gene has been transferred to Ltk(-) cells or that an HSV gene product has caused the expression of a previously repressed cellular enzyme.

Animals↗

Protection of vaccinia from heat inactivation by nucleotide triphosphates.

The presence of adenosine triphosphate, guanosine triphosphate, cytosine triphosphate, or uridine triphosphate reduced the rate of inactivation of vaccinia when heated at 50 C. The virus-associated nucleoside triphosphate phosphohydrolases (adenosine triphosphatase, guanosine triphosphatase, cytosine triphosphatase, and uridine triphosphatase) and ribonucleic acid polymerase were also protected from heat inactivation by these compounds. These obervations are best explained by postulating that ribonucleoside triphosphates bind to enzymes in the virus particle, and that these enzyme-substrate complexes are more resistant to thermal denaturation than are the enzymes without their substrates. The kinetics of heat inactivation of the vaccinia ATP phosphohydrolase activity is biphasic, suggesting that there are two proteins in the vaccinia particle that have this enzyme activity but they have different kinetics of heat inactivation. Any of the vaccinia-associated nucleotide phosphohydrolase activities are protected from heat inactivation by the presence of any one of the respective nucleoside triphosphates. This observation suggests that there is a single enzymatic site in vaccinia that is able to react with any ribonucleoside triphosphate.

Adenosine Triphosphatases↗

Interpretation of tracer data: significance of the number of terms in specific activity functions.

It has already been shown that the number of pools in an open system in the steady state cannot be determined from the number of exponential terms in the specific activity function of a pool, even if the data were free from experimental error. However, some information is conveyed by the number of exponential terms. The information is different depending upon whether the data are obtained from the pool into which the tracer is introduced or from another pool. In the latter case, the number of exponential terms is shown to indicate the maximum number of intermediate pools involved in the shortest path of transfer of material from the injected pool to the pool in question. With regard to the former case, this paper is restricted to functions with two exponential terms and shows which systems of n pools (n >/= 2) are consistent with such data. Consequently, biexponential experimental curves can be interpreted in terms of models consisting of an unrestricted number of pools in which each pool is defined in terms of fast mixing. The generalization to cases of functions with more than two exponential terms can be carried out in a similar manner.

Mathematics↗