Variability in the Proportion and Type of Subunits in Lupin Storage Globulins

1975 ◽  
Vol 2 (1) ◽  
pp. 29 ◽  
Author(s):  
JM Gillespie ◽  
RJ Blagrove
Keyword(s):  
Protein Structure ◽  
Electrophoretic Mobility ◽  
Relative Proportion ◽  
Genetic Selection ◽  
Molecular Size ◽  
The Other ◽  
Subunit Composition ◽  
Molecular Weights ◽  
Species Specific ◽  
Conglutin Γ

The seeds of 12 species of lupin were examined and were found to contain two major globulins, conglutins α and β, while some contained a third minor globulin, conglutin �. There were considerable differences between species in the electrophoretic mobility and proportions of conglutins α and β, and in their subunit composition in terms of the number of components, their molecular weights and the importance of disulphide bonding between them. However, the electrophoretic behaviour and subunit composition of conglutins α and β did appear to be species-specific. Conglutin γ, on the other hand, did not seem to vary in molecular size or electrophoretic mobility within this genus. The 18 cultivars of Lupinus angustifolius examined appeared to be more closely related in terms of the number and size of subunits, although variations were apparent in the relative proportion of these subunits, especially with wild types. It is suggested that this variability in the protein structure of lupin globulins may provide evidence that substantial changes can be induced by genetic selection in the composition of these proteins without upsetting their structure-function relations.

scholarly journals Prebiotic Combinations Effects on the Colonization of Staphylococcal Skin Strains

2020 ◽  
Vol 9 (1) ◽  
pp. 37
Author(s):  
Silvia Di Lodovico ◽  
Franco Gasparri ◽  
Emanuela Di Campli ◽  
Paola Di Fermo ◽  
Simonetta D’Ercole ◽  
...  
Keyword(s):  
Biofilm Formation ◽  
Commensal Bacteria ◽  
The Other ◽  
Bacteriostatic Effect ◽  
Skin Microbiota ◽  
Relevant Effect ◽  
Planktonic Phase ◽  
Species Specific ◽  
Biomass Quantification ◽  
General Reduction

Background: An unbalanced skin microbiota due to an increase in pathogenic vs. commensal bacteria can be efficiently tackled by using prebiotics. The aim of this work was to identify novel prebiotic combinations by exerting species-specific action between S. aureus and S. epidermidis strains. Methods: First, the antimicrobial/antibiofilm effect of Xylitol-XYL and Galacto-OligoSaccharides–GOS combined with each other at different concentrations (1, 2.5, 5%) against S. aureus and S. epidermidis clinical strains was evaluated in time. Second, the most species-specific concentration was used to combine XYL with Fructo-OligoSaccharides–FOS, IsoMalto-Oligosaccharides–IMO, ArabinoGaLactan–LAG, inulin, dextran. Experiments were performed by OD600 detection, biomass quantification and LIVE/DEAD staining. Results: 1% XYL + 1% GOS showed the best species-specific action with an immediate antibacterial/antibiofilm action against S. aureus strains (up to 34.54% ± 5.35/64.68% ± 4.77) without a relevant effect on S. epidermidis. Among the other prebiotic formulations, 1% XYL plus 1% FOS (up to 49.17% ± 21.46/37.59% ± 6.34) or 1% IMO (up to 41.28% ± 4.88/36.70% ± 10.03) or 1% LAG (up to 38.21% ± 5.31/83.06% ± 5.11) showed antimicrobial/antibiofilm effects similar to 1% XYL+1% GOS. For all tested formulations, a prevalent bacteriostatic effect in the planktonic phase and a general reduction of S. aureus biofilm formation without loss of viability were recorded. Conclusion: The combinations of 1% XYL with 1% GOS or 1% FOS or 1% IMO or 1% LAG may help to control the balance of skin microbiota, representing good candidates for topic formulations.

scholarly journals Codon harmonization reduces amino acid misincorporation in bacterially expressed P. falciparum proteins and improves their immunogenicity

AMB Express ◽  
2019 ◽  
Vol 9 (1) ◽  
Author(s):  
Neeraja Punde ◽  
Jennifer Kooken ◽  
Dagmar Leary ◽  
Patricia M. Legler ◽  
Evelina Angov
Keyword(s):  
Protein Structure ◽  
Amino Acid ◽  
Codon Usage ◽  
Dna Sequences ◽  
Structural Integrity ◽  
Host Cells ◽  
Loss Of Function ◽  
Species Specific ◽  
And Function ◽  
The Impact

Abstract Codon usage frequency influences protein structure and function. The frequency with which codons are used potentially impacts primary, secondary and tertiary protein structure. Poor expression, loss of function, insolubility, or truncation can result from species-specific differences in codon usage. “Codon harmonization” more closely aligns native codon usage frequencies with those of the expression host particularly within putative inter-domain segments where slower rates of translation may play a role in protein folding. Heterologous expression of Plasmodium falciparum genes in Escherichia coli has been a challenge due to their AT-rich codon bias and the highly repetitive DNA sequences. Here, codon harmonization was applied to the malarial antigen, CelTOS (Cell-traversal protein for ookinetes and sporozoites). CelTOS is a highly conserved P. falciparum protein involved in cellular traversal through mosquito and vertebrate host cells. It reversibly refolds after thermal denaturation making it a desirable malarial vaccine candidate. Protein expressed in E. coli from a codon harmonized sequence of P. falciparum CelTOS (CH-PfCelTOS) was compared with protein expressed from the native codon sequence (N-PfCelTOS) to assess the impact of codon usage on protein expression levels, solubility, yield, stability, structural integrity, recognition with CelTOS-specific mAbs and immunogenicity in mice. While the translated proteins were expected to be identical, the translated products produced from the codon-harmonized sequence differed in helical content and showed a smaller distribution of polypeptides in mass spectra indicating lower heterogeneity of the codon harmonized version and fewer amino acid misincorporations. Substitutions of hydrophobic-to-hydrophobic amino acid were observed more commonly than any other. CH-PfCelTOS induced significantly higher antibody levels compared with N-PfCelTOS; however, no significant differences in either IFN-γ or IL-4 cellular responses were detected between the two antigens.

scholarly journals Species-Specific Segregation of Gender-Associated Mitochondrial DNA Types in an Area Where Two Mussel Species (Mytilus edulis and M. trossulus) Hybridize

Genetics ◽  
1996 ◽  
Vol 143 (3) ◽  
pp. 1359-1367 ◽  
Author(s):  
Carlos Saavedra ◽  
Donald T Stewart ◽  
Rebecca R Stanwood ◽  
Eleftherios Zouros
Keyword(s):  
Mytilus Edulis ◽  
The Other ◽  
Allozyme Analysis ◽  
Mussel Species ◽  
Species Origin ◽  
Species Pairs ◽  
Nuclear Background ◽  
Species Specific ◽  
Dna Types ◽  
Fertile Hybrids

Abstract In each of the mussel species Mytilus edulis and M. trossulus there exist two types of mtDNA, the F type transmitted through females and the M type transmitted through males. Because the two species produce fertile hybrids in nature, F and M types of one may introgress into the other. We present the results from a survey of a population in which extensive hybridization occurs between these two species. Among specimens classified as “pure” M. edulis or “pure” M. trossulus on the basis of allozyme analysis, we observed no animal that carried the F or the M mitotype of the other species. In most animals of mixed nuclear background, an individual's mtDNA came from the species that contributed the majority of the individual's nuclear genes. Most importantly, the two mtDNA types in post-F1 male hybrids were of the same species origin. We interpret this to mean that there are intrinsic barriers to the exchange of mtDNA between these two species. Because such barriers were not noted in other hybridizing species pairs (many being even less interfertile than M. edulis and M. trossulus), their presence in Mytilus could be another feature of the unusual mtDNA system in this genus.

Specific binding of acrosome-reaction-inducing substance to the head of starfish spermatozoa

Zygote ◽  
1993 ◽  
Vol 1 (2) ◽  
pp. 121-127 ◽  
Author(s):  
Akira Ushiyama ◽  
Takeo Araki ◽  
Kazuyoshi Chiba ◽  
Motonori Hoshi
Keyword(s):  
Acrosome Reaction ◽  
Specific Binding ◽  
Molecular Size ◽  
Polystyrene Latex ◽  
Anterior Region ◽  
Head Region ◽  
Signal Molecule ◽  
Jelly Coat ◽  
Plot Analysis ◽  
Species Specific

In the starfish, spermatozoa undergo the acrosome reaction upon encountering the jelly coat of eggs. A highly sulphated glycoprotein in the jelly coat is called acrosome-reaction-inducing substance (ARIS) because it is the key signal molecule to trigger the acrosome reaction. The activity of ARIS is mainly attributed to its sulphate and saccharide residues. The extremely large molecular size and speciesspecific action of ARIS suggest the presence of a specific ARIS receptor on the sperm surface, but no experimental evidence for the receptor has been presented. We therefore measured specific binding of ARIS and its pronase digest (P-ARIS), which retains the full activity of ARIS, to homologous spermatozoa by using fluorescien-isothiocyanate-labelled ARIS and125 I-labelled P-ARIS, respectively. The spermatozoa had the ability to bind ARIS, as well as P-ARIS, specifically. The binding was species-specific, and mostly localised to the head region of spermatozoa. Scatchard plot analysis indicated the presence of one class of ARIS receptor on the surface of acrosome-intact speramatozoa. Furthermore, the specific binding of P-ARIS to the anterior region of sperm heads was microscopically confirmed by using P-ARIS conjugated to polystyrene latex beads with intense fluorescence. It is concluded that starfish spermatozoa have a specific receptor for ARIS on the surface of the anterior region of heads.

scholarly journals OSMOTIC PRESSURE STUDY OF PROTEIN FRACTIONS IN NORMAL AND IN NEPHROTIC SUBJECTS

1939 ◽  
Vol 69 (6) ◽  
pp. 819-831 ◽  
Author(s):  
Jaques Bourdillon
Keyword(s):  
Osmotic Pressure ◽  
Normal Serum ◽  
The Other ◽  
Protein Fractions ◽  
Molecular Weights ◽  
Other Hand ◽  
Normal Albumin

In serum of patients with nephrosis both albumin and globulin showed by osmotic pressure nearly double the molecular weights of normal albumin and globulin. In the urines of such patients, on the other hand, both proteins showed molecular weights lower even than in normal serum. The colloidal osmotic pressures were measured by the author's method at such dilutions that the van't Hoff law relating pressures to molecular concentrations could be directly applied. For the albumin and globulin of normal serum the molecular weights found were 72,000 and 164,000 respectively, in agreement with the weights obtained by other methods.

scholarly journals THE ABSORPTION OF PROTEIN SOLUTIONS FROM THE PULMONARY ALVEOLI

1937 ◽  
Vol 66 (4) ◽  
pp. 449-458 ◽  
Author(s):  
Cecil K. Drinker ◽  
Madeleine Field Warren ◽  
Margaret MacLanahan
Keyword(s):  
Thoracic Duct ◽  
Horse Serum ◽  
Molecular Size ◽  
The Other ◽  
Immunological Methods ◽  
Protein Solutions ◽  
Blood Capillaries ◽  
Egg Albumin ◽  
Pulmonary Alveoli ◽  
The Right

Horse serum, crystallized hemoglobin, and crystallized egg albumin have been injected into the lung alveoli of dogs in which the entrances of the right lymphatics have been tied and the thoracic duct cannulated. Samples of blood and lymph have been taken following this injection. Only after several hours in the case of the horse serum and hemoglobin have these proteins been detected by immunological methods and invariably they have appeared first in the blood. Egg albumin also enters the blood capillaries, but much more rapidly than the other two proteins, due probably to the smaller molecular size.

Vocal Learning of Japanese and Rhesus Monkeys

Behaviour ◽  
1989 ◽  
Vol 109 (3-4) ◽  
pp. 191-199 ◽  
Author(s):  
Nobuo Masataka ◽  
Kazuo Fujita
Keyword(s):  
Rhesus Monkeys ◽  
Japanese Monkey ◽  
Species Difference ◽  
Vocal Learning ◽  
The Other ◽  
Playback Experiments ◽  
Biological Mothers ◽  
Japanese Monkeys ◽  
The Cross ◽  
Species Specific

AbstractForaging vocalizations given by Japanese and rhesus momkeys reared by their biological mothers differed from each other in a single parameter. Calls made by a Japanese monkey fostered by a rhesus female were dissimilar to those of conspecifics reared by their biological mothers, but similar to those of rhesus monkeys reared by their biological mothers, and the vocalizations given by rhesus monkeys fostered by Japanese monkey mothers were dissimilar to those of conspecifics reared by their biological mothers, but similar to those of Japanese monkeys reared by their biological mothers. Playback experiments revealed that both Japanese and rhesus monkeys distinguished between the calls of Japanese monkeys reared by their biological mothers and of the cross-fostered rhesus monkeys on one hand, and the vocalizations of rhesus monkeys reared by their biological mothers and of the cross-fostered Japanese monkey on the other hand. Thus, production of species-specific vocalizations was learned by each species, and it was the learned species-difference which the monkeys themselves discriminated.

Immune responses of Texel sheep to excretory/secretory products of adult Haemonchus contortus

Parasitology ◽  
1994 ◽  
Vol 108 (3) ◽  
pp. 351-357 ◽  
Author(s):  
H. D. F. H. Schallig ◽  
M. A. W. van Leeuwen ◽  
W. M. L. Hendrikx
Keyword(s):  
Immune Response ◽  
Immune Responses ◽  
Haemonchus Contortus ◽  
Lymphocyte Proliferation ◽  
The Other ◽  
Proliferation Index ◽  
Serum Samples ◽  
Immunoblotting Analysis ◽  
Molecular Weights ◽  
Secretory Products

SUMMARYThe excretory/secretory (E/S) products of adult Haemonchus contortus comprise of at least 15 polypeptides with molecular weights ranging from 10 to > 100 kDa. These E/S products induce an immune response in infected Texel sheep, as demonstrated by specific IgGI levels and a significant lymphocyte proliferation index. Moreover, immunoblotting analysis revealed that sera of primary H. contortus-infected sheep specifically recognize a 24 kDa E/S product. In addition, sera of challenged sheep react strongly with a 15 kDa E/S product. The other E/S products of H. contortus showed immunoreactivity with serum samples of Haemonchus-infected sheep as well as with samples of sheep harbouring other trichostrongylid infections. These cross-reacting epitopes are the main cause of the lack of specificity of an E/S material- based ELISA. This ELISA can differentiate Haemonchus infections from Nematodirus battus infections, but not from Ostertagia circumcincta or Trichostrongylus colubriformis infections.

Effect of extractant and molecular size on the optical and chemical properties of soil humic acids

Soil Research ◽  
1969 ◽  
Vol 7 (3) ◽  
pp. 229 ◽  
Author(s):  
JHA Butler ◽  
JN Ladd
Keyword(s):  
Molecular Weight ◽  
Amino Acid ◽  
Humic Acids ◽  
Gel Filtration ◽  
Chemical Properties ◽  
Molecular Size ◽  
Carboxyl Content ◽  
Peptide Bonds ◽  
Molecular Weights ◽  
Amino Acid Contents

Humic acids extracted from soil with sodium pyrophosphate have greater proportions of lower molecular weight material, less acid-hydrolysable amino acid nitrogen contents, but greater carboxyl contents and extinction values (260 and 450 nm) than humic acids extracted subsequently from the same sample with alkali. Humic acids extracted with alkali from fresh soil samples have intermediate values. Extinction values at 260 nm are directly correlated with carboxyl contents for a given soil. Different crop histories have no significant effect on the measured properties of the extracted humic acids. An alkali-extracted humic acid has been fractionated by gel filtration into seven fractions of different nominal molecular weight ranges. As the molecular weights of the fractions increase, both aliphatic C-H (based on infrared absorption at 2900 cm-1) and acid-hydrolysable amino acid contents increase, whereas extinction values at 260 nm and carboxyl contents decrease. The infrared spectra of the high molecular weight fractions have peaks at 1650 and 1510 cm-1 which correlate with acid-hydrolysable amino acid contents and which correspond to amide I and II bands of peptide bonds. Alkaline hydrolysis to split peptide bonds eliminates both these peaks. The spectra also have peaks at 1720 and 1210 cm-1 which correlate with the carboxyl content.

scholarly journals Trypanosoma cruzi: identification of specific epimastigote antigens by human immune sera

1989 ◽  
Vol 84 (3) ◽  
pp. 309-314 ◽  
Author(s):  
M. G. Morgado ◽  
J. Ivo-dos-Santos ◽  
R. T. Pinho ◽  
E. Argüelles ◽  
J. M. Rezende ◽  
...  
Keyword(s):  
Visceral Leishmaniasis ◽  
Trypanosoma Cruzi ◽  
Western Blot ◽  
Chagas Disease ◽  
Cross Reactivity ◽  
Cross Reaction ◽  
The Other ◽  
Molecular Weights ◽  
Human Visceral Leishmaniasis ◽  
Human Immune

Soluble antigens from epimastigotes of Trypanosoma cruzi were analyzed by western blot in terms of their reactivity with sera from patients with Chagas' disease. In addition, sera from patients with visceral (AVL) and tegumentar leishmaniasis (ATL) were also tested in order to identify cross-reactivities with Trypanosoma cruzy antigens. Twenty eight polypeptides with molecular weights ranging from 14 kDa to 113 kDa were identified with sera from Chagas' disease patients. An extensive cross-reactivity was observed when sera from human visceral leishmaniasis were used, while only a slight cross-reaction was observed with sera from tegumentar leishmaniasis. On the other hand, 10 polypeptidesspecifically reacting with sera from Chagas' disease patients were identified. Among them, the antigens with molecular weights of 46 kDa and 25 kDa reacted with all sera teste and may be good candidates for specific immunodiagnosis of Chagas' disease.

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