Specific cleavage of Sendai virus nucleocapsid protein subunits during virus storage. 1975

L M Popa, and R Repanovici, and I Samuel, and R Portocală

The alteration of whole Sendai virus and especially of its nucleocapsid polypeptides, during storage of the virus at 4 degree C in the allantoic fluids in which it was cultivated, has cultivated, has been studied by sodium dodecyl sulfate gel electrophoresis. During virus storage the nucleocapsid protein subunits with a molecular weight of 60,000 and the putative inner envelope protein with a molecular weight of 38,000 were mainly affected. Both virus components were partially degraded to smaller components. Examination of nucleocapsids isolated from "stored" virus showed that, in addition to the 60,000-molecular weight polypetide component, a smaller polypeptide component with a molecular weight of 46,000 appeared. The relative proportion of the small component increased with the storage period: a kind of specific conversion of large to small components occurred during storage. Since viruses kept in the absence of allantoic fluids revealed no similar modifications of their polypeptides, we concluded that a cellular component present in the allantoic fluids - very likely of enzymatic nature - is responsible for the observed cleavage of virus polypeptides.

UI MeSH Term Description Entries
D008970 Molecular Weight The sum of the weight of all the atoms in a molecule. Molecular Weights,Weight, Molecular,Weights, Molecular
D010222 Parainfluenza Virus 1, Human A species of RESPIROVIRUS also called hemadsorption virus 2 (HA2), which causes laryngotracheitis in humans, especially children. Hemadsorption Virus 2,Human parainfluenza virus 1,Para-Influenza Virus Type 1,Parainfluenza Virus Type 1,Para Influenza Virus Type 1
D010455 Peptides Members of the class of compounds composed of AMINO ACIDS joined together by peptide bonds between adjacent amino acids into linear, branched or cyclical structures. OLIGOPEPTIDES are composed of approximately 2-12 amino acids. Polypeptides are composed of approximately 13 or more amino acids. PROTEINS are considered to be larger versions of peptides that can form into complex structures such as ENZYMES and RECEPTORS. Peptide,Polypeptide,Polypeptides
D012034 Refrigeration The mechanical process of cooling. Cold Chain,Chain, Cold,Chains, Cold,Cold Chains
D001826 Body Fluids Liquid components of living organisms. Body Fluid,Fluid, Body,Fluids, Body
D002213 Capsid The outer protein protective shell of a virus, which protects the viral nucleic acid. Capsids are composed of repeating units (capsomers or capsomeres) of CAPSID PROTEINS which when assembled together form either an icosahedral or helical shape. Procapsid,Prohead,Capsids,Procapsids,Proheads
D003470 Culture Media Any liquid or solid preparation made specifically for the growth, storage, or transport of microorganisms or other types of cells. The variety of media that exist allow for the culturing of specific microorganisms and cell types, such as differential media, selective media, test media, and defined media. Solid media consist of liquid media that have been solidified with an agent such as AGAR or GELATIN. Media, Culture
D005321 Extraembryonic Membranes The thin layers of tissue that surround the developing embryo. There are four extra-embryonic membranes commonly found in VERTEBRATES, such as REPTILES; BIRDS; and MAMMALS. They are the YOLK SAC, the ALLANTOIS, the AMNION, and the CHORION. These membranes provide protection and means to transport nutrients and wastes. Fetal Membranes,Extra-Embryonic Membranes,Extra Embryonic Membranes,Extra-Embryonic Membrane,Extraembryonic Membrane,Fetal Membrane,Membrane, Extra-Embryonic,Membrane, Extraembryonic,Membrane, Fetal,Membranes, Extra-Embryonic,Membranes, Extraembryonic,Membranes, Fetal
D012367 RNA, Viral Ribonucleic acid that makes up the genetic material of viruses. Viral RNA
D014764 Viral Proteins Proteins found in any species of virus. Gene Products, Viral,Viral Gene Products,Viral Gene Proteins,Viral Protein,Protein, Viral,Proteins, Viral

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