Pepsin TOPICAL

Medicinal Uses. One of the earliest medicinal applications of the thiol proteases was the use of fig latex as an anthelmintic agent 16, 17). In more recent times papain has been used as a digestive aid in the treatment of dyspepsia and gastric distress. Its usefulness in this respect derives from the fact that papain remains active under acid conditions and is resistant to attack by pepsin. The intraperitoneal injection of sterile solutions of papain has proved to be effective in preventing post-operative adhesions. Papain is sometimes referred to as a T io-logical scalpel because of its specific proteolytic action on dead tissue without affecting live tissue. For this reason it serves as a very useful debridement in the treatment of bums and the removal of scar tissue. When used in combination with antibiotics, it has proved to be effective for topical treatment of ulcerating and infected lesions. 

If you think about this, it becomes obvious that any major changes in the cellular pH value could seriously upset everything. Most of the proteins are tuned to operate well just on the alkaline side of neutrality, i.e. at pH values of 7.35-7.45. (Exceptions are those proteins that are designed to work in a special acidic niche, like pepsin in the stomach or the various hydrolytic enzymes in the cell s lysosomes Topic 23.) But how can the body maintain a constant pH value when it is constantly carrying out activities that are tending to change the pH Anaerobic metabolism produces lactic acid. Ketogenesis produces acetoacetic and /d-hydroxybutyric acids. Above all, however, cellular aerobic respiration produces CO2, which dissolves in... 

The key to the problem seems then to be the measurement of the enzymatic releasability of protein-bound LAL, as mentioned by Slump (1978). Little on this topic can be found in the literature. Using a closed system (pepsin-pancreatin and pepsin-pronase-prolidase-aminopeptidase), Slump (1978) found an LAL release with treated soybean of 3% (1.3 g LAL/16 g N), and of 2% with treated casein (5.5 g LAL/16 g N content) or 0.5% (1.0 g LAL/16 g N content). Using a different vitro digestion system, Finot et al. (1978) reported a 27% release of LAL from alkali-treated lactalbumine. 

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