scholarly journals Evaluation of the Taxonomic Relationship of Micrococcus cryophilus, Branhamella catarrhalis, and Neisseriae by Comparative Polyacrylamide Gel Electrophoresis of Soluble Proteins

1974 ◽  
Vol 24 (2) ◽  
pp. 172-176 ◽  
Author(s):  
R. H. FOX ◽  
D. E. McCLAIN
1979 ◽  
Author(s):  
C Cierniewski ◽  
T Krajewski ◽  
E Janiak

Various studies on the interaction of immobilized mammalian fibrinogen and fibrin monomers with some fibrinogen derivatives demonstrated the presence of two sets of polymerization sites in the mammalian fibrinogen molecule. We obtained the same results while investigating the fibrinogen molecules of other classes of vertebrates /Pisces. Amphibia. Aves/. Despite significant differences among their subunit structures, all of them contain polymerization sites homologous to mammalian counterparts. Moreover, due to great functional similarity, fibrinogen or fibrin monomers of the analyzed species of Pisces. Amphibia. Aves and Mammalia interacted in a specific way with immobilized pig fibrin monomers or fibrinogen, respectively. Using these pig affinity adsorbents, fibrinogen and fibrin monomers of different vertebrates were isolated directly from plasma and analyzed by SDS polyacrylamide gel electrophoresis. Polypeptide compositions of eluted proteins were identical to those obtained for corresponding fibrinogen preparations isolated by cold-ethanol fractionation method. It appears to indicate that the nature of polymerization sites in vertebrate fibrinogens is alike.


1979 ◽  
Author(s):  
C.S. Ciernlewski ◽  
T. Krajewski ◽  
E. Janiak

Various studies on the interaction of immobilized mammalian fibrinogen and fibrin monomers with some fibrinogen derivatives demonstrated the presence of two sets of polymerisation sites In the mammalian fibrinogen molecule. We obtained the same results while investigating the fibrinogen molecules of other classes of vertebrates /Pisces, Amphibia, Aves/. Despite significant differences among their subunit structures, all of them contain polymerization sites homologous to mammalian counterparts. Moreover, due to great functional similarity, fibrinogen or fibrin monomers of the analyzed species of Pisces, Amphibia, Ayes and Mammalia interacted in a specific way with Immobilized pig fibrin monomers or fibrinogen, respectively. Using these pig affinity adsorbents, fibrinogen and fibrin monomers of different vertebrates were isolated directly from plasma and analyzed by SDS Polyacrylamide gel electrophoresis. Polypeptide compositions of eluted proteins were identical to those obtained for corresponding fibrinogen preparations isolated by cold-ethanol fractionation method. It appears to indicate that the nature of polymerization sites in vertebrate fibrinogens is alike.


1974 ◽  
Vol 52 (12) ◽  
pp. 1143-1153 ◽  
Author(s):  
D. Suria ◽  
C. C. Liew

Non-histone chromatin proteins were isolated from rat-liver nuclei by three different methods, and defined as (I) phenol-soluble proteins, (II) SDS-soluble proteins and (III) proteins not adsorbed by cation-exchange chromatography. About 62–70% of chromatin proteins were recovered from the total nuclear proteins. The yield of non-histone chromatin proteins varied from 17 to 26% of chromatin proteins, depending on the method used. The amino-acid composition of these proteins showed that they are acidic in nature. Their phosphorus content was found to be 0.9, 1.1, and 1.4%, respectively, according to method I, II, or III. In-vivo pulse-labelling experiments indicated that chromatin proteins were highly labelled with 3H-acetate and 32P-phosphoric acid. In particular, the specific activities of 32P incorporation were higher in all non-histone chromatin proteins isolated as compared with histones. One-dimensional SDS–polyacrylamide gel electrophoresis showed that at least 26 similar fractions can be detected in the samples prepared by these three methods.The similarity of some of the proteins obtained from methods I and III was further confirmed by fractionation of the non-histone chromatin proteins in an isoelectro-focusing system followed by a second-dimensional SDS–polyacrylamide gel electrophoresis. It was found that more than 100 components could be identified. However, some minor variations of the non-histone chromatin proteins were detected by this system. The differences in proteins isolated by these methods are mainly quantitative rather than qualitative. The methods examined are not specific for the fractionation of a certain class of non-histone chromatin proteins.


1976 ◽  
Vol 22 (2) ◽  
pp. 309-312 ◽  
Author(s):  
R. R. B. Russell ◽  
I. J. McDonald

In an attempt to elucidate the relation between Micrococcus cryophilus, Neisseria caviae, Neisseria ovis, and Branhamella catarrhalis, fractions derived from outer membranes of a strain of each organism were examined for protein composition by SDS – polyacrylamide gel electrophoresis. Micrococcus cryophilus outer membrane protein showed extensive similarities to that of N. ovis and contained a heat-modifiable protein which behaved almost identically with the corresponding bands previously shown to exist in N. caviae and N. oris. Branhamella catarrhalis protein was distinctly different from those of M. cryophilus and the two 'false neisserias' N. caviae and N. oris.


1971 ◽  
Vol 49 (8) ◽  
pp. 1293-1297 ◽  
Author(s):  
Gilles Pelletier ◽  
Robert Hall

Buffer-soluble proteins extracted from six morphologically different isolates of Verticillium were separated by polyacrylamide gel-electrophoresis. Protein patterns from the six isolates were different from one another whether extracts were prepared from conidia, from young colonies composed of mycelium and conidia, or from 6-day-old mycelium. However, the nature of the patterns, and therefore the degree of differences among species patterns, was influenced by the types of cells from which the extracts were prepared.Patterns of proteins from V. tricorpus, V. nigrescens, and an isolate of uncertain identity (isolate 2) which produced chlamydospores and dark mycelium were clearly different from one another whether extracts were prepared from conidia or mycelium. In contrast, conidia of V. albo-atrum, of V. dahliae, and of an isolate which did not produce pigmented structures produced very similar patterns which differed by only a few protein bands. This close similarity of patterns supports the view that V. albo-atrum and V. dahliae are genetically closely related.The protein composition of conidia differed from that of mycelium. In V. albo-atrum, spore extracts contained at least three proteins not detected in mycelium extracts. Differences between spores and mycelium were even greater in V. nigrescens and isolate 2. Analysis of V. dahliae showed differences between spores, 3-day-old mycelium, and 6-day-old mycelium.Our results support the view that gel-electrophoresis of proteins is useful as a taxonomic tool provided attention is given to the degree of morphological differentiation of the materials to be compared.


2015 ◽  
Vol 47 (4) ◽  
pp. 371-378 ◽  
Author(s):  
W. Lassocińsk ◽  
J. S. Knypl

Four major and 14 minor protein bands were detected when total salt soluble proteins of soybean (Glycine max cultivar Warszawska) seed were subjected to polyacrylamide gel electrophoresis under nondissociating conditions, and 16 protein bands were detected under dissociating conditions. Molecular weights of three major protein fractions in PAGE SDS were determined for around 18 500, 36 000 and 80 000 daltons.


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