9 research outputs found
Morphological and Isozyme Variation in Natural Populations of the Genus Medicago L. Prospected in Northern Algeria
As part of the evaluation and enhancement of genetic resources, morphological and isozyme variability within and among 169 accessions, representing 14 species of the genus Medicago L. collected in northern Algeria, was assessed using twelve quantitative traits and two enzymatic systems. Phenotype frequencies were scored in six enzyme zones to determine isozyme variability within and among populations. The data analysis resolved a high level of genetic diversity. Ten morphometric characteristics contributed to the discrimination of the species. The relationship between the collection site environment and phenotypic characteristics was also studied. Esterase (EST) enzyme system was more polymorphic than glutamate oxaloacetate transaminase (GOT) system. Were scored 2 zones with 10 bands and 21 phenotypes for GOT (glutamate oxaloacetate transaminase) and 4 zones with 22 bands and 71 phenotypes for EST (esterase) Polymorphism index and Jaccard’s genetic distances revealed the existence of a high genetic diversity within and among the studied populations. The annual species M. polymorpha presented an intraspecific polymorphism index of 0.57, which was higher than all other species indices. Clustering of the species based on isozyme markers was in agreement with taxonomic criteria and showed no significant correlation with morphological characteristics. Conservation programs should take into account the level of genetic diversity within and between populations revealed by isozyme markers
Physical and chemical properties of the acid protease from Onopordum acanthium: Comparison between electrophoresis and HPLC of degradation casein profiles
A protease was extracted by grinding, precipitation and gel filtration from Onopordum acanthium flowers. The physicochemical study of the enzyme showed an optimum pH of 4, a temperature of 40°C and kinetic parameters of 12.25 mM-1 for KM and 1329.6 UmL-1 for Vmax. The inhibition by pepstatin indicated that it is an aspartyl-protease (APs). Zymogram showed that the protease has a monomeric structure and a molecular mass (MM) of 45 kDa. The hydrolysis of α, β and Κ- and whole casein by the protease was evaluated using electrophoresis and HPLC; the profiles showed many similarities between the vegetal protease action and that of industrial chymosin. So, the properties of the protease studied and the quality of its action showed its effectiveness and relevance of its use as a milk clotting enzyme which leads to a better use of extract of flowers O. acanthium as a locally substitute for rennet.Keywords: Aspartic protease, Onopordum acanthium, purification, characterization, casein hydrolysi
Diversity of Seven Glutenin and Secalin Loci within Triticale Cultivars Grown in France
Although the endosperm storage protein of hexaploid triticale have already been analysed, the allelic diversity of glutenins and secalins remains to be described. Analysis by SDS-PAGE of the majority of hexaploid triticales (69 cultivars) grown in France allowed to identify 36 alleles at seven loci: Glu-A1, Glu-B1, Glu-R1, Gli-R2, Glu-B2, Glu-A3 and Glu-B3. Glu-B1 and Glu-B3 loci were the most polymorphic with 9 alleles each. On the basis of allelic frequencies at the seven loci, genetic distances between hexaploid triticales grouped according to their origins revealed two groups: winter triticales mostly originating from European germplasm and spring triticales essentially of CIMMYT origin. Comparison of allele frequencies between hexaploid triticale cultivars and a world collection of bread (Triticum aestivum) and durum (Triticum durum) wheat was investigated at Glu-A1 and Glu-B1: only a significant association was found for Glu-A1 alleles (?2 = 2.26, p =0.36) between triticale and bread wheat
Milk-clotting properties and specific hydrolysis of caseins of the acid protease extracted from Scolymus maculatus flowers
A milk-clotting acid protease was extracted from the flowers of an Asteraceae; a widespread plant traditionally used in Algeria, Scolymus maculatus. The enzyme was purified 40 fold using ammonium sulfate fractionation followed by exclusion chromatography. The estimation of the molecular mass of the protease by SDS-PAGE electrophoresis gave a weight of 45 kDa and Zymogram analysis revealed only one proteolytic band. The enzyme inhibition at 99% by pepstatin-A 5 mM proved that it is an aspartic proteinase; EDTA and iodoacetamide had no effect. The milk coagulation activity of this protease was optimal at pH 5 and 60°C, the rennet strength (RS) of the extract increased with calcium concentrations and was saturated at 50 mM. The enzyme exhibited hydrolytic activity toward κ-casein, α s -and β-casein. These results indicated that Scolymus maculatus protease has technological effects similar to that of the chymosin; the enzyme could be used in cheese making as a substitute for rennet
Tyrosinase Inhibitory Ability and In Vitro, In Vivo Acute Oral and In Silico Toxicity Evaluation of Extracts Obtained from Algerian Fir (<i>Abiesnumidica</i> de Lannoy ex CARRIERE) Needles
This study was designed to evaluate the tyrosinase inhibitory effect, in vitro, in vivo, and in silico toxicity of fractions isolated from A. numidica de Lannoy needles. The cytotoxicity of extracts was examined against Artemia salina larvae, while the toxicity of these extracts was tested by acute oral toxicity in mice; by administration of a dose of 2000 mg/kg b.w A. numidica leaves extracts. The blood samples were collected from the eye orbital sinus for further analysis of biochemical parameters. The absorption, distribution, metabolism, elimination, and toxicity (ADMET) properties were identified by the pkCSM web server. The data stated that ethyl acetate (EA) presented strong anti-tyrosinase apt. The results reported that ethyl acetate extract exhibited a strong inhibitory capacity against A. salina larvae with LD50 of 75.004 µg/mL. The data also showed that no mortality occurred, and no toxicity symptoms were observed in mice. The biochemical parameters revealed that both extracts significantly affected the hepatic profile by increasing ALT, AST, and alkaline phosphatase. Histopathological tests also confirmed that both fractions were toxic at this concentration on hepatic and renal tissues, with necrosis observed. The toxicity of molecules in silico revealed no effect on all examined biomolecules.It can be concluded that this plant was toxic on the liver and renal profiles and tissues at the dose studied
Mutations of the aurora kinase C gene causing macrozoospermia are the most frequent genetic cause of male infertility in Algerian men
Klinefelter syndrome and Y-chromosomal microdeletion analyses were once the only two genetic tests offered to infertile men. Analyses of aurora kinase C (AURKC) and DPY19L2 are now recommended for patients presenting macrozoospermia and globozoospermia, respectively, two rare forms of teratozoospermia particularly frequent among North African men. We carried out genetic analyses on Algerian patients, to evaluate the prevalence of these syndromes in this population and to compare it with the expected frequency of Klinefelter syndrome and Y-microdeletions. We carried out a retrospective study on 599 consecutive patients consulting for couple infertility at the assisted reproduction unit of the Ibn Rochd Clinique, Constantine, Algeria. Abnormal sperm parameters were observed in 404 men. Fourteen and seven men had typical macrozoospermia and globozoospermia profiles, respectively. Molecular diagnosis was carried out for these patients, for the AURKC and DPY19L2 genes. Eleven men with macrozoospermia had a homozygous AURKC mutation (79%), corresponding to 2.7% of all patients with abnormal spermograms. All the men with globozoospermia studied (n = 5), corresponding to 1.2% of all infertile men, presented a homozygous DPY19L2 deletion. By comparison, we would expect 1.6% of the patients in this cohort to have Klinefelter syndrome and 0.23% to have Y-microdeletion. Our findings thus indicate that AURKC mutations are more frequent than Klinefelter syndrome and constitute the leading genetic cause of infertility in North African men. Furthermore, we estimate that AURKC and DPY19L2 molecular defects are 10 and 5 times more frequent, respectively, than Y-microdeletions