Comparison of isolates in the Chaetomium aureum species group by esterase isoenzyme analysis

1987 ◽  
Vol 65 (1) ◽  
pp. 198-201 ◽  
Author(s):  
Á. Szécsi ◽  
S. Tóth
Keyword(s):  
Isoelectric Focusing ◽  
Isoelectric Point ◽  
Soluble Protein ◽  
Species Group ◽  
Diagnostic Markers ◽  
Polyacrylamide Gel ◽  
Isoenzyme Analysis ◽  
Esterase Isoenzyme

Soluble protein extracts from 19 isolates of Chaetomium were subjected to isoelectric focusing in polyacrylamide gel rods. The isoelectric point (pI) values of esterase isoenzymes were determined and the data used to calculate coefficients of similarity. Isolates of C. aureum and C. trilaterale were electrophoretically distinct, whereas isolates of C. confusum, C. humicola, C. rubrogenum, and C. trilaterale were not distinguishable electrophoretically from each other. The profiles A, B, F, and G can be used to distinguish the species of C. atrobrunneum, C. aureum, C. cupreum and C. fusiforme. These results partly agreed with the morphologically based classification of the C. aureum species group. Certain esterase bands were found to be useful as diagnostic markers for differentiating Chaetomium species.

MEASUREMENT OF CANINE PITUITARY PROLACTIN

1973 ◽  
Vol 56 (2) ◽  
pp. 245-NP ◽  
Author(s):  
P. G. SALUJA ◽  
M. GRONOW ◽  
J. M. HAMILTON
Keyword(s):  
Isoelectric Focusing ◽  
Isoelectric Point ◽  
Gel Electrophoresis ◽  
Polyacrylamide Gel ◽  
Brilliant Blue ◽  
Coomassie Brilliant Blue ◽  
Ovine Prolactin ◽  
Pituitary Prolactin ◽  
Coomassie Brilliant

SUMMARY Isoelectric focusing in polyacrylamide gel followed by staining with Coomassie brilliant blue was used for the densitometric estimation of ovine prolactin standard and canine pituitary prolactin. The results were compared with those obtained by conventional polyacrylamide gel electrophoretic procedures and isoelectric focusing was found to be a valid technique for the estimation of prolactin and to offer greater technical convenience. The mobility of ovine and canine prolactin was similar in isoelectric focusing and gel electrophoresis. The isoelectric point of ovine and canine prolactin was found to be 6·17 and 6·61 respectively. Constant levels of prolactin were found in the pituitaries of bitches at oestrus.

Isoelectric focusing of insulin, 125I-insulin and the 125I-insulin-antibody complex

1979 ◽  
Vol 44 (6) ◽  
pp. 1828-1834
Author(s):  
Asja Šiševa ◽  
Jiřina Slaninová ◽  
Tomislav Barth ◽  
Stephan P. Ditzov ◽  
Luben M. Sirakov
Keyword(s):  
Isoelectric Focusing ◽  
Polyacrylamide Gel ◽  
The Other ◽  
Insulin Antibody ◽  
Isoelectric Points ◽  
Antibody Complex ◽  
And Storage ◽  
Acid Region ◽  
Three Components

Isoelectric focusing on polyacrylamide gel columns of three native crystalline commercial preparations of insulin and 125I-labelled insulin was carried out. All the compounds studied contained three components of different isoelectric points. The largest fraction, having pI 5.60 ± 0.05, was common to all preparations. The other two fractions were situated in the acid region of pH between pI 4.5 and 5.2. The presence of these fractions is explained by the contamination of crystalline insulins by proinsulin and by the formation of des-amido derivatives during the dissolving and storage of insulin samples, and, in case of labelled insulin, also by the presence of heavily iodinated insulin and contaminating components. The isoelectric focusing of the complex 125I-insulin-antibody showed a peak of radioactivity having pI 6.15 ± 0.05.

Discovery of New Genera Challenges the Subtribal Classification of Tok-Tok Beetles (Coleoptera: Tenebrionidae: Sepidiini)

2021 ◽  
Vol 5 (2) ◽  
Author(s):  
Olivia M Gearner ◽  
Marcin J Kamiński ◽  
Kojun Kanda ◽  
Kali Swichtenberg ◽  
Aaron D Smith
Keyword(s):  
Dna Sequences ◽  
Species Group ◽  
Phylogenetic Placement ◽  
Darkling Beetles ◽  
Species Groups ◽  
Taxonomic Groups ◽  
Inference Methods ◽  
A New Species ◽  
Coleoptera Tenebrionidae

Abstract Sepidiini is a speciose tribe of desert-inhabiting darkling beetles, which contains a number of poorly defined taxonomic groups and is in need of revision at all taxonomic levels. In this study, two previously unrecognized lineages were discovered, based on morphological traits, among the extremely speciose genera Psammodes Kirby, 1819 (164 species and subspecies) and Ocnodes Fåhraeus, 1870 (144 species and subspecies), namely the Psammodes spinosus species-group and Ocnodes humeralis species-group. In order to test their phylogenetic placement, a phylogeny of the tribe was reconstructed based on analyses of DNA sequences from six nonoverlapping genetic loci (CAD, wg, COI JP, COI BC, COII, and 28S) using Bayesian and maximum likelihood inference methods. The aforementioned, morphologically defined, species-groups were recovered as distinct and well-supported lineages within Molurina + Phanerotomeina and are interpreted as independent genera, respectively, Tibiocnodes Gearner & Kamiński gen. nov. and Tuberocnodes Gearner & Kamiński gen. nov. A new species, Tuberocnodes synhimboides Gearner & Kamiński sp. nov., is also described. Furthermore, as the recovered phylogenetic placement of Tibiocnodes and Tuberocnodes undermines the monophyly of Molurina and Phanerotomeina, an analysis of the available diagnostic characters for those subtribes is also performed. As a consequence, Phanerotomeina is considered as a synonym of the newly redefined Molurina sens. nov. Finally, spectrograms of vibrations produced by substrate tapping of two Molurina species, Toktokkus vialis (Burchell, 1822) and T. synhimboides, are presented.

scholarly journals Mechanism of methaemoglobin reduction by human erythrocytes

1980 ◽  
Vol 188 (2) ◽  
pp. 535-540 ◽  
Author(s):  
A Tomoda ◽  
M Ida ◽  
A Tsuji ◽  
Y Yoneyama
Keyword(s):  
Methylene Blue ◽  
Isoelectric Focusing ◽  
Rate Constants ◽  
Time Course ◽  
Reaction Rate ◽  
Polyacrylamide Gel ◽  
Human Erythrocytes ◽  
Redox Potentials ◽  
Reaction Rate Constants ◽  
Beta 2

The time course of methaemoglobin reduction in human erythrocytes treated with nitrite was studied at pH 7.4, 37 degrees C, in the presence or absence of Methylene Blue, and the changes in methaemoglobin, intermediate haemoglobins and oxyhaemoglobin during the reaction were analysed by isoelectric-focusing on Ampholine/polyacrylamide-gel plates. In both cases, with or without the dye, the intermediate haemoglobins were found to be present at (alpha 3+beta 2+)2 and (alpha 2+beta 3+)2 valency hybrids from their characteristic position on electrophoresis, but amounts changed consecutively with time. The amount of (alpha 3+beta 2+)2 was always greater than that of the (alpha 2+beta 3+)2 valency hybrid. This result is explained by the differences in redox potentials between alpha- and beta-chains in methaemoglobin tetramer. It was concluded that methaemoglobin was reduced in human erythrocytes through these two different pats: methaemoglobin leads to k+3 (alpha 2+beta 3+)2 leads to k+3 oxyhaemoglobin. The reaction rate constants k'+1 (= k+1+k+3) and k'+2(=k+2+k+4) were estimated from the changes in each component methaemoglobin, intermediate haemoglobins [(alpha 3+beta 2+)2+(alpha 2+beta 3+)2] and oxyhaemoglobin.

scholarly journals A Comparative Study of Plasma Proteins from Twenty-Nine Species of Albatrosses And Petrels (Order Procellariiformes)

2021 ◽  
Author(s):  
◽  
Peter C Harper
Keyword(s):  
Plasma Proteins ◽  
Species Group ◽  
Reference Points ◽  
Evolutionary Significance ◽  
Group Level ◽  
Family Level ◽  
Phylogenetic Conservatism ◽  
History Of ◽  
Biochemical Research

<p>The plasma proteins of 29 species of albatrosses and petrels were electrophoretically separated in acrylamide gels to clarify relationships at the species-group to family-group levels. Little in the resulting data from 472 birds seriously contests the present classification of the Procellariiformes; much of the biochemical evidence supports, confirms, and clarifies the proposals of conventional taxonomic methodology. The biochemical data give fresh insights into the interrelationships of procellariiform taxa, and highlight intriguing new problems. Sex, season, age, and other sources of non-genetic protein variation are insignificant for taxonomic purposes. Proteins of comparable value include the transferrins, some α and β globulins, albumins, prealbumins, and non-specific esterases. Genetic variations in the mobility of these proteins are useful at the genus-group level and below. Other proteins are monomorphic at genus and family level, and three are monomorphic in both number and mobility throughout the Procellariiformes; these are useful reference points for calibrating samples on different gels. One conspicuous α protein is absent in the Hydrobatidae but present in all other families; the implications of this are discussed. Polymorphic proteins at the population or species level were not detected; this conspicuous phylogenetic conservatism is discussed with regard to its possible evolutionary significance. Following a summary of the protein data; three categories of, defined probability statements, based on the biochemical and other evidence, allow speculative comment on the evolutionary relationships and history of the taxa within the Procellariiformes. The value of further biochemical research into the marine birds is emphasised.</p>

scholarly journals ANALYSIS OF SHEEP HEMOGLOBINS BY ISOELECTRIC FOCUSING IN POLYACRYLAMIDE-GEL

1983 ◽  
Vol 1983 (11) ◽  
pp. 39-42
Author(s):  
Masaharu KOTANI ◽  
Kenji TSUNODA ◽  
Tatsuro SHIMAOKA
Keyword(s):  
Isoelectric Focusing ◽  
Polyacrylamide Gel

scholarly journals Reductive alkylation of ribosomes as a probe to the topography of ribosomal proteins*

1974 ◽  
Vol 143 (3) ◽  
pp. 607-612 ◽  
Author(s):  
Graham Moore ◽  
Robert R. Crichton
Keyword(s):  
Escherichia Coli ◽  
Protein Complex ◽  
Gel Electrophoresis ◽  
Ribosomal Proteins ◽  
Polyacrylamide Gel Electrophoresis ◽  
Polyacrylamide Gel ◽  
Two Dimensional ◽  
Reductive Alkylation ◽  
Lysine Residues

Escherichia coli ribosomes were treated with a number of different aldehydes of various sizes in the presence of NaBH4. After incorporation of either 3H or 14C, the ribosomal proteins were separated by two-dimensional polyacrylamide-gel electrophoresis and the extent of alkylation of the lysine residues in each protein was measured. The same pattern of alkylation was observed with the four reagents used, namely formaldehyde, acetone, benzaldehyde and 3,4,5-trimethoxybenzaldehyde. Every protein in 30S and 50S subunits was modified, although there was considerable variation in the degree of alkylation of individual proteins. A topographical classification of ribosomal proteins is presented, based on the degree of exposure of lysine residues. The data indicate that every protein of the ribosome has at least one lysine residue exposed at or near the surface of the ribonucleo-protein complex.

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