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Biomedical subjects

D C Shaw

Publications and source records attributed to D C Shaw.

At least 91 records · Page 5Linked to original sources
PubMed1976

Translation in vitro of artificially produced fragments of a tobamovirus genome.

Particles of the U2 strain of tobacco mosaic virus (TMV) were partly disassembled by SDS, treated with RNases and then phenol, and yielded RNA molecules one quarter to half the size of the intact virus genome. These molecules, when translated in vitro, produced the coat protein of the virus. Reassembly experiments indicated that the active messenger molecules were those that most rapidly reassembled with coat protein; the rate of reassembly was greatly diminished by treatment with spleen phosphodiesterase. Particles of sunnhemp mosaic virus (the bean strain of TMV) resist disassembly by detergent much more than those of the U2 strain of TMV.

Cell-Free System↗
PubMed1976

Mixed infection with two tobamoviruses: the formation of particles containing the coat protein messenger RNAs of either virus.

Plants mixedly infected with the U2 strain of tobacco mosaic virus (T2MV) and sunnhemp mosaic virus (SHMV) and grown at 35 degrees, yield particles of the same modal lengths (300 and 40 nm) as those found in plants singly infected with SHMV, but not in plants infected with T2MV, which yield only the long particles. At least some of the particles produced in mixedly infected plants contain coat proteins of both viruses. When RNAs from these particles are translated in vitro the coat proteins of both viruses are produced, although when a mixture of RNAs from particles of SHMV and T2MV, grown separately, are translated in vitro only SHMV protein is produced. These and other results suggest that the short particles produced in mixedly infected plants contain both coat protein messengers.

Antigens, Viral↗
PubMed1972

Radiochemical determination of a unique sequence around the reactive serine residue of a di-isopropyl phosphorofluoridate-sensitive plant carboxypeptidase and a yeast peptidase.

Phaseolain, a carboxypeptidase from French-bean leaves, and a partially purified peptidase from baker's yeast are inhibited by reaction with di-isopropyl phosphorofluoridate. Radioactive di-isopropyl [(32)P]phosphorofluoridate was used to show that the site of reaction is a unique serine residue and that the sequence of amino acids adjacent to the reactive serine is Glu-Ser-Tyr. This sequence is different from those of other ;serine' enzymes previously reported and, for phaseolain, represents an unequivocal example of a ;serine' carboxypeptidase.

Amino Acid Sequence↗