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Mechanistic bases for adverse vaccine reactions and vaccine failures. Adv Vet Med. 1999;41:681-700. doi: 10.1016/s0065-3519(99)80053-6. PMID: 9890054; PMCID: PMC7149317.
Deoxyribonuclease I (usually called DNase I), is an endonuclease of the DNase family coded by the human gene DNASE1. [5] DNase I is a nuclease that cleaves DNA preferentially at phosphodiester linkages adjacent to a pyrimidine nucleotide, yielding 5'-phosphate-terminated polynucleotides with a free hydroxyl group on position 3', on average producing tetranucleotides.
It is a recombinant human deoxyribonuclease I (rhDNase), an enzyme which selectively cleaves DNA. [3] Dornase alfa hydrolyzes the DNA present in sputum/mucus and reduces viscosity in the lungs, promoting improved clearance of secretions. [3] It is produced in Chinese hamster ovary cells. [3]
Deoxyribonuclease II (DNase II) is also known as acid deoxyribonuclease because it has optimal activity in the low pH environment of lysosomes where it is typically found in higher eukaryotes. Some forms of recombinant DNase II display a high level of activity in low pH in the absence of divalent metal ions, similar to eukaryotic DNase II. [7]
DNA vaccine and Gene therapy techniques are similar. DNA vaccines have been introduced into animal tissues by multiple methods. In 1999, the two most popular approaches were injection of DNA in saline: by using a standard hypodermic needle, or by using a gene gun delivery. [31] Several other techniques have been documented in the intervening years.
A marker vaccine is a vaccine which allows for immunological differentiation (or segregation) of infected from vaccinated animals, and is also referred to as a DIVA (or SIVA) vaccine [Differentiation (or Segregation) of infected from vaccinated animals] in veterinary medicine. [1]
The following is a list of notable proteins that are produced from recombinant DNA, using biomolecular engineering. [1] In many cases, recombinant human proteins have replaced the original animal-derived version used in medicine. The prefix "rh" for "recombinant human" appears less and less in the literature.
Analysis of crossover junction endodeoxyribonucleases from bacteriophages (T7 endonuclease I), bacteria (RuvC), fungi (GEN1) and humans (hMus81-Eme1) have revealed that the enzymes function in dimers, [11] and part of the resolution reaction takes place in a partially dissociated enzyme-substrate intermediate.