Pancreatine

Pancrease Pancreatectomy Pancreatic a-amylase Pancreatic dornase Pancreatic elastase Pancreatic hypertrophy Pancreatic lipase Pancreatin [8049-47-6]... 

Upases. The idea of using Upases in the wash process dates back to 1913 when O. Rn hm suggested a dding pancreatin [8049-47-6] to detergent formulations. Many patents have demonstrated that Upases can improve the removal of fatty stains when used in powder and liquid detergents, special presoakers, or other cleaning agents. Intense research activity is also reflected in the literature (43—45). 

Another subclass of proteases attacks internal peptide bonds and Hberates large peptide fragments. Bromelain, a plant protease derived from the stem of the pineapple plant, can even produce detectable semm proteolysis after oral adrninistration (180). Oral therapy with bromelain significantly reduces bmising that stems from obstetrical manipulations (181). Bromelain—pancreatin combinations have been more effective in digestive insufficiency compared to either pancreatin or placebo (182,183). Bromelain may also enhance the activity of antibiotics, especially tetracycline, when adrninistered concurrently (184). 

Entozyme 18/100 Digestive enymes pancreatin/pepsin/bile salts Robins... 

Pancrease 30/100 pancreatin/pepsin/bile salts McNeil... 

Tlozyme 77/250 pancreatin/pepsin/bile salts Adtia... 

Hi-Vegi-Lip 15/100 pancreatin/hpase/protease/amylase Freeda... 

Digestalin 3/100 extract/ceUulase/glutamic acid pancreatin/pepsin/papain/activated Vortech... 

Donnazyme 20/100 nyltoloxamine pancreatin/pepsin/homatropine/hyoscyamine/atropin Robins... 

FIGURE 8.13 SEC of casein hydrolyzates. Numbers above the peaks refer to the number of amino acid residues in the typical peptide in the indicated fraction. Column PolyHEA, 200 X 9.4 mm 5 /zm, 200 A. Flow rate 0.5 ml/min. Mobile phase 50 mtA Formic acid. Detection A250. Samples (A) Pancreatin hydrolyzate and (B) tryptic hydrolyzate. (Adapted from Ref. 29 with permission from Silvestre et of. Copyright 1994, American Chemical Society.)... 

Digestive Enzymes pancreatin Creon, Digepepsin, 1-2 tablets PO with meals... 

The enzymes pancreatin and pancrelipase, which are manufactured and secreted by the pancreas, are responsible for the breakdown of fats, starches, and proteins. These enzymes are necessary for the breakdown and digestion of food. Both enzymes are available as oral supplements. 

Recently, an enzymatic method was reported to recover the three main components of industrial shrimp waste (protein, chitin, and astaxanthin) using treatments with alcalase and pancreatin. The first enzyme was more efficient in increasing the recovery of protein from 57.5 to 64.6% and of astaxanthin from 4.7 to 5.7 mg/lOO g of dry waste. 

Somatostatin. Somatostatin is an endogenous peptide hormone involved in e.g. the control of the release of Somatomedin, Insulin and Pancreatin. Due to its biological role, Somatostatin has a very low biological stability. The half-life in the rabbit after intravenous administration has been determined to approximately 90 seconds in this investigation. After sc or im administration, the apparent half-life is somewhat longer, close to 10 minutes, probably due to the absorption of the peptide from the injection site into the systemic circulation. 

T Dahl, ILT Sue, A Yum. The effect of pancreatin on the dissolution performance of gelatin-coated tablets exposed to high-humidity conditions. Pharm Res 8 412-414,1991. 

Tryptophane.—In an 8-1. (2-gal.) bottle is placed 600 g. of commercial casein (coarse powder), which is then covered with about 3200 cc. of tap water at 370 (Note 1). The bottle is shaken until all of the casein is moistened. A solution of 60 g. of anhydrous sodium carbonate (Note 2) and 6 g. of sodium fluoride (Note 3) in 1 1. of water at 37° is added. A thin paste of 20 g. of commercial pancreatin in roo cc. of water (370) is poured in. The mixture is covered with a layer of toluene (80 cc.), diluted to 6 1., stoppered, shaken thoroughly, and placed in a warm room or bath at 370. 

After four or five days, with daily shakings, most of the casein is in solution and chalky masses of tyrosine begin to separate. After five days, a second dose of 20 g. of pancreatin in 100 cc. of water is added. After twelve days, the bottle is cooled in an ice-box over night and the undissolved material is filtered off (Note 4) and reserved for the preparation of tyrosine. 

Rodriguez et al. [68] studied the stability of niclosamide in artificial gastric and intestinal juices. The gastric juice contained sodium chloride and hydrochloric acid with or without pepsin. The intestinal juice contained sodium phosphate with or without pancreatin. Niclosamide was incubated with the juices at 37°C for 6 h. The remaining intact drug and its degradation products (2-chloro-4-nitroaniline, 5-chlorosalicylic acid) were extracted with chloroform/methanol (5 1) and determined by TLC and HPLC. The drug was stable in these media for at least for 6 h. 

Pancreatin is a pancreatic extract usually obtained from the pancrease of slaughterhouse animals. It contains a mixture of enzymes, principally amylase, protease and lipase, and, thus, exhibits a broad digestive capability. It is administered orally mainly for the treatment of pancreatic insufficiency caused by cystic fibrosis or pancreatitis. As it is sensitive to stomach acid, it must be administered in high doses or, more usually, as enteric-coated granules or capsules that may be taken directly or sprinkled upon the food prior to its ingestion. Individual digestive activities, such as papain, pepsin or bromelains (proteases), or a-amylase are sometimes used in place of pancreatin. 

Substances to be stored in tightly-closed, light-resistant containers in a cool place, e.g., nitrofurantoin, pancreatin, oxyphenonium bromide. 

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