China
Africa
Explore chapters and articles related to this topic
Dendrimers in Gene Delivery
Published in Neelesh Kumar Mehra, Keerti Jain, Dendrimers in Nanomedicine, 2021
Dnyaneshwar Baswar, Ankita Devi, Awanish Mishra
Gene therapy is a promising technique that focuses on the utilisation of genes to treat or prevent diseases ranging from single gene disorder to multi-gene disorder. The experimental approaches of gene therapy may authorise doctors to treat any diseases by introducing a gene into patient’s cells in place of surgery or drugs (Sung and Kim 2019). Gene therapy looks to alter genes to ameliorate genetic defects and cure genetic diseases. It is one of the most advanced strategies for therapeutic prospects searching for stopping genetic diseases to fight cancer. The basic process of gene therapy is substituting a faulty gene that creates disease with a normal gene and knocking out/deactivating a mutant gene that is working inappropriately (Maguire et al. 2014). Gene therapy in multiple forms will be giving clinical improvements in patients with neuromuscular disease, blindness, haemophilia, cancer and immune deficiencies (Dunbar et al. 2018). Currently, researchers are focusing on the safety of gene therapy, for future studies whether therapy is a safe and effective treatment option for the prevention of diseases such as viral infection, cancer and inherited disorders (Yang et al. 2015).
Ionizing Radiation
Published in Ivan G. Draganić, Zorica D. Draganić, Jean-Pierre Adloff, Radiation and Radioactivity on Earth and Beyond, 2020
Ivan G. Draganić, Zorica D. Draganić, Jean-Pierre Adloff
Genetic mutations are caused by damage to the hereditary material of the cell, i.e., in the chromosomes, which are thread-like constituents of nucleus. They contain genes, the carriers of information which determines the characteristics of daughter cells. Here, radiation-induced damage causes chromosome aberration, involving changes in their number or structure and mutations of the genes themselves. These mutations are of two types: dominant, which concerns the children of persons already affected by radiation, and recessive, which may be dormant for many generations and first becomes manifest in a child whose parents both possess the mutant gene. Many diseases are associated with recessive genes. Since mutant genes are generally recessive, it is assumed that virtually all mutations are harmful. Ionizing radiation increases the rate of mutation and, in the prevailing circumstances, it is to be feared that an increased population of genetically abnormal individuals could appear in future generations.
Some applications of the hypergeometric and Poisson distributions
Published in Henry C. Tuckwell, Elementary Applications of Probability Theory, 2018
In cells changes in genetic (hereditary) material occur which are called mutations. These may be spontaneous or induced by external agents. If mutations occur in the reproductive cells (gametes) then the offspring inherits the mutant genes. In humans the rate at which spontaneous mutations occur per gene is about 4 per hundred thousand gametes (Strickberger, 1968). In the common bacterium E. coli, a mutant variety is resistant to the drug streptomycin. In one experiment, N = 150 petri dishes were plated with one million bacteria each. It was found that 98 petri dishes had no resistant colonies, 40 had one, 8 had two, 3 had three and 1 had four. The average number n̄ of mutants per million cells (bacteria) is therefore n˜=40×1+8×2+3×3+1×4150=0.46.
Purification and biochemical characterization of pullulanase produced from Bacillus sp. modified by ethyl-methyl sulfonate for improved applications
Published in Preparative Biochemistry & Biotechnology, 2023
Oladipo O. Olaniyi, Blessing Oriade, Olusola T. Lawal, Adeyemi O. Ayodeji, Yetunde O. Olorunfemi, Festus O. Igbe
The wild-type and mutant Bacillus sp. pullulanases have optima activity at neutral and alkaline pH 8.0 respectively signifying the conferment of adaptability to pH change by the enzyme produced by the bacterium with the altered genetic make-up. The wild-type bacterial pullulanase exhibited a high relative percentage of enzymatic activity at alkaline pH region suggesting the enzyme to be very much active between neutral and alkaline pH domains. Previous reports from Bacillus sp[10,29] and Klebsiella pneumonia[28] were in agreement with enzymatic optimum pH of wild-type Bacillus sp. pullulanase. Whereas, Pullulanase from Bacillus sp.[50] had an optimum pH activity of 6.0, and white edible mushroom, pH 9.0[27]. The report of Rajaei et al.[51] from Exiguobacterium sp was in accordance with that of mutant Bacillus sp. pullulanase while Bacillus sp Cheorl-Ho[31] had an optimum activity at pH 9.0. The alkalophilic property of the mutant and neutral nature of the wild-type pullulanase make them good candidates for the textile industries, starch saccharification, and also in the laundry for the removal of starchy stains and primer[52].
Evaluation of a single amino acid substitution at position 79 of human IFN-α2b in interferon-receptor assembly and activity
Published in Preparative Biochemistry and Biotechnology, 2019
Samira Talebi, Alireza Saeedinia, Mehdi Zeinoddini, Fathollah Ahmadpour, Majid Sadeghizadeh
Cell growth and IFN-α2b (T79Q) production were determined for stable transfected CHO cells after G418 antibiotic treatment. Expression of IFN-α2b (T79Q) mRNA was shown by RT-PCR (Fig. 2). Expression of IFN-α2b (T79Q) in the level of protein was confirmed, as well as, purified IFN-α2b (T79Q) that determined using Western-blot analysis (Fig. 3). The amino acids sequence of IFN-α2b was obtained from Drug Bank [Accession number: DB00105 (BIOD00066, BTD00066)] and the sequence of IFN-α2b (T79Q) is shown in Fig. 3. The expression yield of IFN-α2b (T79Q) was 10% of total protein in the cell culture. Its concentration was measured 12.33 μg/ml using Bradford technique. After purification, IFN-α2b (T79Q) was found in the 12th fraction with about 90% purity. Its concentration in purified fraction was 30 μg/ml (30 mg/l), and the yield of protein purification was measured (54%). The wild-type protein was used as control versus of the mutant. In all assays, an equal concentration of wild-type and mutant protein was used.
Engineered Alcaligenes sp. by chemical mutagen produces thermostable and acido-alkalophilic endo-1,4-β-mannanases for improved industrial biocatalyst
Published in Preparative Biochemistry & Biotechnology, 2023
Oladipo Oladiti Olaniyi, Ademola Sunday Ajulo, Olusola Tosin Lawal, Victoria Kehinde Olatunji
The wild type and mutant Alcaligenes sp. β-mannanase exhibited maximum stability and retained it’s initial activity at 40 °C after 90 and 60 min respectively. Overall, the wild-type purified enzyme demonstrated relative stability at 30-80 °C with a percentage residual activity of approximately 68-87% but showed declined activity with 39% residual activity at 90 °C after 120 min (Figure 5). β-mannanase of the mutant type maintained its stability between 40 and 90 °C with residual activity of 51-83% after 120 min of incubation (Figure 6).