Trypsin pancreatin

RIVM Stomach Small intestine Oral cavity Gastric juice (pepsin, mucin), pH 2 Intestinal juice (porcine bile, trypsin, pancreatine), pH 7.5 Saliva, pH 6.5 Pb, Cr, Hg As, Cd, 5, 10... 

Cestodes apparently rely entirely on host enzymes for digestion of intermediate cystic stages in the definitive host. Requirements for various species include host pepsin, trypsin, pancreatin and bile salts (21). 

Incubate the embryonic tissue in a trypsin-pancreatin solution (see section 2.2) for 5-10 min or until the endoderm is loosened from the mesoderm. 

Incubate the embryonic fragments in the trypsin-pancreatin solution for 20 min at 37°C. When the mesoderm and ectoderm layers are loosened, separate the tissue layers using glass needles. 

Relevant quality control should not be restricted to the usual triad of activities of pancreas lipase, a-amylase, and trypsin, but should be extended to the content of colipasc, the activities of the two other lipolytic enzymes present in pancreatine (phospholipase Aj and carboxylester lipase), and the dissolution characteristics of enteric-coated preparations as a function of time and pH (Fig. 16). The availability of such information will certainly contribute to a better tailoring of flic management of maldigestion in the individual patient and to a more appropriate correction of the obligate nonphysio logical route of delivery of these enzyme supplements. 

Species Pepsin Trypsin Lipase Pancreatin Bile salt Reference... 

Pancreatic enzymes, preferably trypsin, have been used for the chemical characterisation and identification of many known bioactive peptides. For example, ACE-inhibitory peptides as well as CPPs are most commonly produced by trypsin (Maruyama and Suzuki, 1982 Berrocal et al., 1989). On the other hand, other enzymes and different enzyme combinations of proteinases, including alcalase, chymotrypsin, pancreatin and pepsin, as well as enzymes from bacterial and fungal sources have also been utilised to generate bioactive peptides. Higher yields of CPPs and, particularly, higher amounts of asl-casein f(59-79) in the hydrolysate have been obtained with casein micelles successively digested with pepsin and trypsin... 

Involvement of sperm proteolytic enzymes in fertilization processes has a long history. Perhaps the first definitive observation that sperm proteases affected egg envelopes was that of Yamane in 1935. He demonstrated that an extract of rabbit sperm dispersed the cumulus cells and solubilized the zona pellucida (ZP) or egg envelope of the rabbit egg (1.). The presence of proteases in the sperm extract was presumed by analogy with the dispersing action of the trypsin activity in pancreatin. In 1939, Tyler obtained an extract from sperm of the giant keyhole limpet Meeathura crenulata which dissolved the egg envelope without affecting the egg itself. 

Lipase (Microbial) Activity for Medium- and Long-Chain Fatty Acids, (S3)105 Lysozyme Activity, (S3)106 Maltogenic Amylase Activity, 804 Milk-Clotting Activity, 805 Pancreatin Activity, 805 Pepsin Activity, 807 Phospholipase A2 Activity, 808 Phytase Activity, 808 Plant Proteolytic Activity, 810 Proteolytic Activity, Bacterial (PC), 811 Proteolytic Activity, Fungal (HUT), 812 Proteolytic Activity, Fungal (SAP), 813 Pullulanase Activity, 814 Trypsin Activity, 814 Enzyme Assays, 786 Enzyme-Hydrolyzed (Source) Protein,... 

Recrystallized trypsin (Armour) had no effect on the purified fibers, but commercial grade trypsin effected the dissolution of the fibers when incubated overnight at 37°C. This was apparently due to the presence in the commercial trypsin preparations of pancreatic elastase (Bald and Banga, 1949). When treated for a short time with a partly purified preparation of elastase, obtained from pancreatin, the elastic fibers were eroded to a degree that the smooth cylindrical structure was lost and under the light microscope the fiber appeared to be composed of a pair of intertwined fibrils each approximately 2 n ln diameter. The process of dissolution then accelerated, and in favorable specimens each fibril was seen to resolve into a pair of similarly intertwined members, each with a diameter of approximately 1 ft. These 4 strands were very friable and under Brownian motion rapidly broke up into short beadlike segments and soon disappeared. 

CAS 9001-62-1. Any of a class of enzymes that hydrolyze fats to glycerol and fatty acids. Lipase is abundant in the pancreas but also occurs in gastric mucosa, in the small intestine, and in fatty tissue. It is found in milk, wheat germ, and various fungi. Commercial pancreatin and most trypsin preparations contain lipase. 

A09A A Enzyme Preparations Enzymes can be used therapeutically. Some are of animal origin (from the stomach and pancreas of food animals), some of vegetable origin and others of microbiological origin. Examples of the first type include pepsin and pancreatin, a mixture of amylase, lipase and trypsin (a protease) which catalyses the metabolism of proteins into smaller peptides and amino-acids. Pancreatin is frequently prescribed for patients with cystic fibrosis. 

Insulinase. An enzyme that hydrolyzes insulin and is prepd from hog pancreas Brink, Lewis, U.S. pet. 2,957, -809 (I960 to Merck Co.). May be obtained from commercial pancreatin or trypsin. Even the purified crystals contain large amounts of elastase. Review Thomas, Postgrad. Med. J. Suppl, 49, 940 (1973). 

Pancreatin. Diastase vera Creon Pancrease Pancrex Vet Pankrotanon Zypanar. A substance from the Itesh pancreas of the hog or ox, contg the enzymes amylop-srn, trypsin. and steapsin. It converts not less than 25 times its wt of starch into sol carbohydrates and not less than 25 times its wt of casein into proteoses within 5 mins, (equiv to 130 times in 30 mins.). Its greatest activity is exhibited in neutral or faintly alkaline media mineral acids or excess al-lali hydroxides or carbonates render it inactive. Method of production from cow or pig pancreas Hoek ei at, U.S, pat. 3,223,594 (1965 to N, American Philips). 

Crude and purified proteases derived from the pancreas have a long history of commercial use. Many of the applications employ a cruder form, pancreatin, but some drug applications require purified trypsin. 

The preceding table is the result of experiments made by Lawrow the solution of peptone which he used was 15 per cent, the temperature of the experiment was 40°, and its duration 70 hours. At this concentration, we see that the maximum of plastein obtained corresponds to a trace of HCl, or to a brownish tint of Congo paper. Trypsin and pancreatin furnish plastein even in a neutral medium. The maximum yield is obtained with a very slight alkalinity. 

The first data on the enzymes of the pancreatic juice were furnished by Cl. Bernard in 1855 and Corvisart in 1858. It is to the latter that we owe the name of pancreatin, given to the active constituents of the pancreatic juice. Danilewsky, in 1862, isolated from a maceration of pancreas three enzymes, one amylolytic, a second proteolytic, and finally a third, capable of emulsifying and of saponifying fatty substances. Kiihnc, in 1867, first drew attention to the difference which exists between the chemical action of pepsin and that of the pancreatic enzyme. He showed the production, in this second action, of tyrosin and leucin, and also of those ill-defined residues from the hydrolysis of albuminoids which he called anti-peptones. He then characterized this proteolytic enzyme as a new enzyme, distinct from pepsin, and gave to it the name of trypsin. 

Trypsin, in a dry state, endures very well the effect of a moderate heating. Harlay, by the aid of tyrosinase proved that trypsin, which has been brought to loo , still digests fibrin very easily with the rapid production of tyrosin. Hufner has found the same result for pancreatin. According to Schmidt, trypsin can be heated for an hour and a half at 112° without destroying the active substance. Salkowski even finds that dry trypsin resists the temperature of 160" for an hour and a half, but that it is destroyed at 170°. 

Influence of Salts.—-Relative to the action of chemical agents on trypsin and pancreatin we piossess very contradictory data, which result from the very different conditions under which... 

In all these determinations, there is a very important point on which writers do not often insist enough, and which renders their results but little comparable, namely, the strength of the trypsin used. Achalme recommends a maceration of 5 to 7 per cent of pancreatin made in a physiological solution for 18 to 24 hours at 35°, in the presence of several drops of essence of mustard. The liquid is filtered and distributed in sterilized and sealed pipettes, which are kept in the dark. This trypsin is then tested with respect to its effect on the serum of an adult guinea pig. By using the method of Achalme, just described, a trypsin should be obtained, o.oi c.c. to 0.015 of which (or o.i c.c. to 0.15 c.c. of a i-io dilution) is neutralized by about o.oi c.c. (or o.i c.c. of i-ioo dilution) of guinea-pig serum, or again by 0.015 c.c. of rabbit serum. 

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