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Polyacrylamide gel electrophoresis of the 30S ribosomal proteins derived from six streptomycin resistant strains indicates that each mutation alters the same ribosomal protein (str-r protein). Preliminary data utilizing SDS gels indicates that the str-r protein has a molecular weight between 10,000 and 20,000 daltons. No significant differences could be detected between the molecular weight of the str-r protein when it is derived either from a sensitive or from a resistant strain, including those derived from strains carrying multisite mutations of different genetic size. We have estimated the size of the multisite str-r mutations to be less than 30 base pairs. Two factor crosses with str-r markers in the trans position demonstrate recombination frequencies expected of closely linked, intragenic markers although cotransfer frequencies, of these same markers from the cis position, are very low. It is concluded that the cotransfer frequencies represent a marker effect and possible explanations are discussed. A reinterpretation of the genetic map of the pneumococcal str-r locus is presented.
Mol Gen Genet 1977 May 20
PMID:A comparison of the genetic and physical size of the streptomycin resistance locus in Pneumococcus. 1 58

Electrophoresis of ribosomal proteins according to Kaltschmidt and Wittmann, 1970a, b (pH 8.6/pH 4.5 urea system) yielded 29 proteins for the small subunits and 35 and 37 proteins for the large subunits of Krebs II ascites and HeLa ribosomes, respectively. Analysis of the proteins according to a modified technique by Mets and Bogorad (1974) (pH 4.5/pH 8.6 SDS system) revealed 28 and 29 proteins in the small subunits and 37 and 38 proteins in the large subunits of Krebs II ascites and HeLa ribosomes. The molecular weights of the individual proteins were determined by: 1. "three-dimensional" gel electrophoresis; 2. two-dimensional gel electrophoresis at pH 4.K/pH 8.6 in SDS. The molecular weights for 40S proteins ranged from 10,000 to 39,000 dalton (number average molecular weight: 21,000). The molecular weights for the 60S proteins ranged from 14,000 to 44,000 dalton (number average molecular weight: 23,000) using the "three-dimensional" technique. A molecular weight range from 10,000 to 38,000 dalton (number average molecular weight: 21,000) was obtained for the 40S subunits, whereas the molecular weights for the 60S ribosomal proteins (average molecular weight: 26,000) ranged from 12,000 to 69,000 dalton using the pH 4.5/pH 8.6 SDS system. The molecular weights Krebs II ascites and HeLa ribosomal proteins are compared with those obtained by other authors for different mammalian species.
Mol Gen Genet 1978 Apr 17
PMID:Characterisation of ribosomal proteins from HeLa and Krebs II mouse ascites tumor cells by different two-dimensional polyacrylamide gel electrophoresis techniques. 2 16

The sedimentation of radiolabelled 22 nm hepatitis B surface antigen particles was unaffected by treatment with either trypsin or SDS alone, but combined treatment disrupted the particulate nature of the radiolabelled material. Considerable antibody binding activity by the group-specific determinant (a) was preserved after combined SDS and trypsin treatment but was released from the bulk of the radiolabelled protein; gel filtration indicated an approximate mol. wt. of 5000 to 15000 for the released antibody binding material. This material was precipitated by concanavalin A, suggesting the presence of carbohydrate. Its serological activity was remarkably resistant to boiling and to proteolytic digestion, but was partially sensitive to treatment with 0-01 M-periodate or with mixed carbohydrases and neuraminidase, and was greatly reduced by treatment with reducing agent. These data suggest that the stability of the a determinant is due to the structure of the antibody binding site itself, rather than to involvement in the quaternary structure of the particle, and that intact disulphide bonds and carbohydrate, closely related to the antibody binding site, are necessary for the full expression of serological acitivity.
J Gen Virol 1976 Oct
PMID:Tryptic cleavage of antibody binding sites from hepatitis B surface antigen particles. 6 23

Human leukocyte interferon, purified approximately 1000-fold by affinity chromatography on immobilized anti-interferon globulins and SDS-Sephadex filtration, was resolved into one major and one minor component by adsorption chromatography on hydroxylapatite and electrophoresis in polyacrylamide gels. These components were indistinguishable in their capacity to protect bovine, porcine and murine cells, and the antiviral activities of both were equally susceptible to reduction by beta-mercaptoethanol. They were neutralized to the same degree of rabbit anti-leukocyte interferon but were not neutralized by rabbit antifibroblast interferon serum. Mice immunized with either component developed antibodies to both but failed to form antibodies against human fibroblast interferon. Our present evidence indicates that the two components posses at most only minor structural and antigenic dissimilarities.
J Gen Virol 1977 May
PMID:Biological properties of human leukocyte interferon components. 6 14

Of the three major proteins associated with the rabies virus membrane, only the glycoprotein was found to be located on the external surface of the virus membrane. Glycoprotein prepared by treatment of rabies virus with Triton X-100 and purified by isoelectric focusing was found to be homogeneous with respect to size and isoelectric point. This material, which is free of phospholipids, is able to protect in vaccination experiments against a lethal challenge infection with rabies virus. The apparent mol. wt. of this component isolated under non-denaturing conditions is approx. 400000. The same material analysed by SDS polyacrylamide gel electrophoresis (PAGE) was found to consist solely of polypeptide chains of the G protein (mol. wt. 80000). A minor glycoprotein (gp 50), detected by PAGE of the Triton X-100 released material, appeared to be a breakdown product of the G-protein. Therefore the detergent released material represents homopolymers of the G-protein. Whether the antigenic determinants reside on the monomeric subunit or are a property of the polymeric form of the G-protein is discussed.
J Gen Virol 1978 Jul
PMID:Isolation and purification of a polymeric form of the glycoprotein of rabies virus. 8 Apr 43

Five phages which are morphologically similar to coliphage T7 but attack other host bacteria have been compared to T7 and to its relative, T3, by the following criteria: (a) cross-reactivity with antisera against T7 and T3, (b) DNA base sequence homologies, as determined by the C0t technique, (c) synthesis of two phage-coded enzymes: RNA polymerase and SAMase, (d) patterns of phage-directed protein synthesis, as determined by SDS-polyacrylamide gel electrophoresis of phage coat subunits. As judged by all these criteria, Pseudomonas phage PX3 is not related to T7; thus, morphological similarity was attributed to convergent evolution. The other phages, i.e. Serratia phage IV, Psuedomonas phage gh-1, Citrobacter phage ViIII and Klebsiella phage No. 11, were considered to be related to T7 on the basis of similarities in the patterns of phage-coded proteins and because, early after infection, these phages induced, as T7 does, an RNA polymerase which specifically transcribes the DNA of thehomologous phage. Phages IV and No. 11 also induced the early synthesis of SAMase (previously only known to occur upon T3 infection). With the exception of phage IV, however, DNA base sequence homologies with T7 or T3 seem to be poor or non-existent. The tested phages, again with the exception of phage IV, did not react with antiserum against T3 or T7. It is concluded that a particular pattern of phage-directed protein synthesis (as characterized by polyacrylamide gel electrophoresis and enzyme tests) may provide evidence for phylogenetic relationships between phages, even in cases where other criteria, such as genetic recombination, serological cross-reaction, and DNA base sequence homologies, fail to indicate relatedness.
J Gen Virol 1979 Apr
PMID:The strategy of infection as a criterion for phylogenetic relationships of non-coli phages morphologically similar to phage T7. 9 Jan 10

Measles virus Edmonston strain was purified by ultrafiltration followed by two successive sedimentations through sucrose. Purified virus retained infectivity and, when used as an immunogen, elicited high titred antibody to measles antigens by conventional serology. The measles preparations were examined by SDS-PAGE followed by staining. In addition, following PAGE, the purity of these preparations was assessed immunochemically using antisera directed to measles and host cell antigens. The results of these studies demonstrate the utility of the purification method for the preparation of milligram quantities of relatively pure measles virus.
J Gen Virol 1979 Jun
PMID:Purification of measles virus with preservation of infectivity and antigenicity. 9 Jan 18

Representative isolates of the paramyxoviruses duck/Hong Kong/75 and duck/Mississippi/75 were shown to be serologically closely related by haemagglutination and neuraminidase inhibition tests. The structural polypeptides of these viruses were also shown to be similar. For each of the isolates tested, polyacrylamide gel electrophoresis in the presence of SDS revealed a similar polypeptide pattern consisting, under reducing conditions, of seven polypeptides with apparent mol. wt. ranging from 46000 to 190000. Each virus had two glycosylated polypeptides with apparent mol. wt. of 56000 and 71000 to 72000 under reducing conditions and 62000 to 63000 and 135000 to 142000 under non-reducing conditions.
J Gen Virol 1979 Sep
PMID:Antigenic and structural relationships between avian paramyxoviruses isolated from ducks in Hong Kong and Mississippi, U.S.A. 9 19

The constituents of LS antigen from cells infected with vaccinia virus and with cowpox virus were compared by immunoprecipitation and SDS-polyacrylamide gel electrophoresis (SDS-PAGE). Antiserum to the LS antigen from cells infected with vaccinia virus reacted with at least five polypeptides in cells infected with either virus. Four of these polypeptides were similar sizes in cells infected with the two viruses. However, one major polypeptide with a mol. wt. of about 100 000 (100 K) detected in cells infected with vaccinia virus was not found in cells infected with cowpox virus. Conversely, a polypeptide with a mol. wt. of about 60 000 (60K) was detected only in cells infected with cowpox virus.
J Gen Virol 1979 Dec
PMID:Comparative studies on LS antigens induced by vaccinia and cowpox viruses. 9 51

Pulse-chase experiments after synchronous initiation of translation indicate that the larger Venzuelan equine encephalomyelitis (VEE) virus membrane glycoprotein E2, is derived by proteolytic cleavage of the precursor, PE2. The structural proteins of VEE virus strains representing each of the antigenic subtypes and varieties have been compared by discontinuous SDS-polyacrylamide gel electrophoresis. Nucleocapsid proteins of all isolates were similar in size (mol. wt. 35 to 36 X 10(3). The mol. wt. of E1 varied from 48 to 51 X 10(3) and the mol. wt. of E2 glycoproteins ranged from 53 to 59 X 10(3). Pixuna virus contained a third envelope glycoprotein of 59 X 10(3) mol. wt. in addition to the two major glycoproteins of mol. wt. 53 X 10(3) and 48 X 10(3) respectively. The isoelectric points (pI) of E1 and E2 for all VEE strains studied were approx. 7 and 9 respectively. Both glycoproteins of TC-83 virus induced precipitating antibodies which reacted only with the homologous purified E1 and E2 glycoproteins. Antibodies to E2 protein of each virus neutralized virus infectivity and inhibited the agglutination of goose erythrocytes by virions. Haemagglutination-inhibition tests using antisera to E2 glycoproteins of prototype viruses, representing each of the antigenic subtypes and varieties, differentiated the viruses into subtypes I, II, III and IV with subtype I divided into variants 1AB, 1C, 1D and 1E.
J Gen Virol 1979 Sep
PMID:Biochemical and antigenic comparison of the envelope glycoproteins of Venezuelan equine encephalomyelitis virus strains. 11 35


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