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M D Summers

Publications and source records attributed to M D Summers.

100 records · Page 6Linked to original sources

Granulosis virus deoxyribonucleic acid: a closed, double-stranded molecule.

Studies on deoxyribonucleic acid purified from the granulosis virus of Trichoplusia ni have revealed the presence of a closed, double-stranded superhelix which sediments at 95S relative to relaxed circles (74S) and linear (60S) forms. Molecular weight estimates show that this insect virus deoxyribonucleic acid has a size of 100 x 10(6) daltons.

Centrifugation, Density Gradient↗

Pathway of infection of mosquito iridescent virus. I. Preliminary observations on the fate of ingested virus.

Mosquito iridescent virus (MIV) is ingested in large amounts by first- and second-instar Aedes taeniorhynchus larvae without causing a high rate of infection. Electron microscope studies have been undertaken to determine the fate of ingested virus. Preliminary observations suggest that most, if not all, ingested particles are degraded shortly after entering the midgut. MIV and other virus particles employed in this study were apparently unable to penetrate the peritrophic membrane; consequently, none was observed inside, or in contact with, midgut epithelial cells.

Aedes↗

Comparative studies of baculovirus granulins and polyhedrins.

Granulins and polyhedrins from five baculoviruses exhibit similar chemical and physical properties. Although similarities are demonstrated, it has been shown that each of the proteins is different and apparently specific to a given virus. The granulins and polyhedrins exhibit a major polypeptide component of an estimated molecular weight of 28,000. Alkaline protease activity has been detected in each preparation. N-terminal analyses reflect differences between granulins and polyhedrins studied: granulosis virus = Asx, and nuclear polyhedrosis virus = Glx. Two-dimensional high-voltage electrophoresis of highly purified granulin and polyhedrin preparations reveals relatedness as well as differences among the proteins as assessed by electrophoretic migration patterns.

Amino Acids↗