Neurotoxin produced by fermentation of clostridium botulinum type B. The protein exists in noncovalent association with hemagglutinin and nonhemagglutinin proteins as a neurotoxin complex. The neurotoxin complex is recovered from the fermentation process and purified through a series of precipitation and chromatography steps.
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The product was first isolated in 1941 from the crude latex derived from the fruit of Carica papaya by squeezing the green papaya while on the plant prior to harvest. It is an extracellular plant cysteine proteinase similar to papain in specificity.
The product is a potent enzyme in gastric juice that digests proteins such as those in meat, eggs, seeds, and dairy products.
Studies on gastric digestion from 1820-1840 led to the discovery of the product as the substance which, in the presence of stomach acid, causes nutrients including meat or coagulated egg whites to dissolve. Soon afterward, it was shown that these protein nutrients were cleaved by the product to products called peptones.
Studies on gastric digestion from 1820-1840 led to the discovery of the product as the substance which, in the presence of stomach acid, causes nutrients including meat or coagulated egg whites to dissolve. Soon afterward, it was shown that these protein nutrients were cleaved by the product to products called peptones.
The product is a biosynthetic form of human deoxyribunuclease I (DNase I) enzyme. It is recombinantly produced in genetically modified CHO cells. The 260-amino acid sequence is identical to the endogenous human enzyme. The product cleaves extracellular DNA to 5´-phosphodinucleotide and 5´-phosphooligonucleotide end products without affecting intracellular DNA.