Identification of Sendai virus neuraminidase and hemagglutinin subunits

Popa, L; Repanovici, R; Samuel, I; D, Smelţ; Portocala, R

doi:10.1016/0014-5793(75)80904-5

Cited by 3 publications

(4 citation statements)

References 10 publications

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“…As it can be seen from this figure, in the "fresh" virus about six polypeptides are found, whose molecular weights and relative distribution are similar to those described by CO-~T~T and DrESSinG (3), MOUNTCASTLE, CO5'IPA-N-S and C~orrIx (6), and Po~'~t et al (8,9).…”

Section: Polypeptide Distribution Found In "Stored" Virussupporting

confidence: 75%

“…The polypeptides with molecular weights of 75,000, 65,000 t and 53,000 (components 1, 2 and 4 in Figure i A) are carbohydrate-containing components (8,9). They correspond to virus proteins 1, 2 and 5 described by ~2¢[OUNTCASTLE et al (6), or to virus proteins 2, 4 and 5 described by Co~T and DVESBERG (3), which are also glycoproteins.…”

Section: Polypeptide Distribution Found In "Stored" Virusmentioning

confidence: 95%

“…Gel c o n c e n t r a t i o n was 10 per cent acrylamide, 0.27 per cent bisacrylamide. Electrophoresis was carried out vertically in glass tubes (9). A t t h e b o t t o m of each figure, t h e eleetrophoregrams of t h e Coomassie Brilliant B l u e -s t a i n e d gels are shown.…”

Section: Polypeptide Distribution Found In "Stored" Virusmentioning

confidence: 99%

“…Virus and nueleocapsid polypcptides were analysed either by the conventional vertical disc eleetrophoresis procedure, using glass tubes of 12 cm with an internal diameter of 6.5 mm (9) or by the flat gel electrophoresis apparatus of AWTAL and ELSON, as previously described (8).…”

Section: Polyacrylamide Gel Electrophoresismentioning

confidence: 99%

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Specific cleavage of Sendai virus nucleocapsid protein subunits during virus storage

Popa¹,

Repanovici²,

Samuel³

et al. 1975

Archives of Virology

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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.

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Section: Polypeptide Distribution Found In "Stored" Virussupporting

confidence: 75%

Section: Polypeptide Distribution Found In "Stored" Virusmentioning

confidence: 95%

Section: Polypeptide Distribution Found In "Stored" Virusmentioning

confidence: 99%

Section: Polyacrylamide Gel Electrophoresismentioning

confidence: 99%

See 2 more Smart Citations

Specific cleavage of Sendai virus nucleocapsid protein subunits during virus storage

Popa¹,

Repanovici²,

Samuel³

et al. 1975

Archives of Virology

Self Cite

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Inhibition of the neuraminidase of paramyxoviruses by halide ions: A possible means of modulating the two activities of the HN protein

et al. 1981

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Variance-corrected Michaelis-Menten equation predicts transient rates of single-enzyme reactions and response times in bacterial gene-regulation

Pulkkinen

Metzler

2015

Sci Rep

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Many chemical reactions in biological cells occur at very low concentrations of constituent molecules. Thus, transcriptional gene-regulation is often controlled by poorly expressed transcription-factors, such as E.coli lac repressor with few tens of copies. Here we study the effects of inherent concentration fluctuations of substrate-molecules on the seminal Michaelis-Menten scheme of biochemical reactions. We present a universal correction to the Michaelis-Menten equation for the reaction-rates. The relevance and validity of this correction for enzymatic reactions and intracellular gene-regulation is demonstrated. Our analytical theory and simulation results confirm that the proposed variance-corrected Michaelis-Menten equation predicts the rate of reactions with remarkable accuracy even in the presence of large non-equilibrium concentration fluctuations. The major advantage of our approach is that it involves only the mean and variance of the substrate-molecule concentration. Our theory is therefore accessible to experiments and not specific to the exact source of the concentration fluctuations.

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Identification of Sendai virus neuraminidase and hemagglutinin subunits

Cited by 3 publications

References 10 publications

Specific cleavage of Sendai virus nucleocapsid protein subunits during virus storage

Specific cleavage of Sendai virus nucleocapsid protein subunits during virus storage

Inhibition of the neuraminidase of paramyxoviruses by halide ions: A possible means of modulating the two activities of the HN protein

Variance-corrected Michaelis-Menten equation predicts transient rates of single-enzyme reactions and response times in bacterial gene-regulation

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