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Pancreatin Activity

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,... [Pg.123]

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). [Pg.295]

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). [Pg.311]

Digestalin 3/100 extract/ceUulase/glutamic acid pancreatin/pepsin/papain/activated Vortech... [Pg.313]

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. [Pg.365]

Nunoura, C. Umezawa, and K. Z0246 Yoneda. Studies on effect of crude drugs on enzyme activities. 1. Influence of cinnamon bark upon protein diges- Z0247 tive action by pancreatin. Shoyaku-gaku Zasshi 1982 36 11-16. [Pg.555]

Pectase was found in plants, both in soluble and non soluble form. It was able to break down pectose into pectinic acid, and was attributed some similarity to diastase. Neither materials could be crystallized (Payen, 1874). Claude Bernard was the first to show lipolytic activity in pancreas in 1856 (Tauber, 1949), and Dobell (1869) found that an extract from pancreas hydrolyzed both fat and starch he gave a procedure for extraction and stabilization and named this preparation pancreatine . [Pg.4]

Exocrine pancreatic insufficiency is most commonly caused by cystic fibrosis, chronic pancreatitis, or pancreatic resection. When secretion of pancreatic enzymes falls below 10% of normal, fat and protein digestion is impaired and can lead to steatorrhea, azotorrhea, vitamin malabsorption, and weight loss. Pancreatic enzyme supplements, which contain a mixture of amylase, lipase, and proteases, are the mainstay of treatment for pancreatic enzyme insufficiency. Two major types of preparations in use are pancreatin and pancrelipase. Pancreatin is an alcohol-derived extract of hog pancreas with relatively low concentrations of lipase and proteolytic enzymes, whereas pancrelipase is an enriched preparation. On a per-weight basis, pancrelipase has approximately 12 times the lipolytic activity and more than 4 times the proteolytic activity of pancreatin. Consequently, pancreatin is no longer in common clinical use. Only pancrelipase is discussed here. [Pg.1330]

Additives in dissolution medium Purified pepsin up to an activity of 750,000 units/lOOOmL or pancreatin up to an activity of 10 USP units/lOOOmL Not specified Polysorbate 80 up to 1.0% w/v ... [Pg.55]

Pancreatic and malt amylases gradually lose their activity in the aqueous dispersions in which they act. As above noted, there is good evidence that this is due to a destructive hydrolysis of the enzyme. The destructive action of water upon enzyme is less pronounced in the presence of substrate, probably because the combination of enzyme with substrate serves to some extent to protect the enzyme from hydrolysis. It is less rapid in solutions of commercial pancreatin and in water extracts of malt than it is in solutions of purified pancreatic and malt amylases, doubtless because of the presence in the former of substances which are products of protein hydrolysis (proteoses, peptones, polypeptids, amino acids) and whose presence therefore tends to retard further protein hydrolysis and thus to protect the enzyme protein from hydrolytic destruction, or at least to diminish the rate at which such deterioration of the enzyme occurs. [Pg.3]

Four major enzyme groups are secreted lipolytic, proteolytic, amylolytic, and nucleic acid splitting enzymes. These pancreatic enzymes, some of which are secreted in multipile forms, possess specificities complementary to die intestinal membrane-bound enzymes (Tabic 1). Fresh, uncontsnkinated pancreatic juice is without proteolytic activity because these enzymes am in the form of inactive zymogens. An important fraction of the calcium in pancreatic juice accompanies the enzymes, especially ct-amylase. Human pancreatic juice is moat dose to that of the pig, with high proportions of lipase and a-amylase in comparison with other mammals [1]. Therefore, pig pancreas extract, pancreatin, has up to now been die oreferred enzvme source for therapeutic tuncreas substitution. [Pg.187]

Figure 4, where the curve is the result of opposite effects of colipase and bile salts. Maximum activities am reached in the range of 5-13 mM bile salts, a concentration aiso present in the duodenum during fat digestion, in me FI method for pancreatin lipase, about 10 mM FIP controlled sodium taurocholate is used. [Pg.194]

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. [Pg.214]

Crews et al. [81] studied cooked cod by means of a two-step in vitro gastrointestinal enzymolysis. For the first step of sample preparation they employed gastric juice (1 percent m/v pepsin, pH = 2.0, in 0.15 mol l-1 NaCl) at 37°C for 4 h. Afterwards a pancreatin-based mixture was added to the sample solution containing 1.5 percent m/v pancreatin, 0.5 percent m/v amylase, and 0.15 percent m/v bile salts in 0.15 mol l-1 NaCl at pH = 6.9 for a further 4 h at 37°C. The relatively short (8 h) enzymatic activity and the lack of enzymes capable of hydrolyzing proteins directly into amino acids resulted in the identification of inorganic Se (IV) only, as no selenoamino acids could be detected. [Pg.608]

The patient also was advised to change his dietary habits by avoiding large meals and eating several smaller or medium meals. He was treated with pancreatin, a medication containing a mixture of porcine pancreatic enzymes, including lipase, amylase, and proteases, with the dosage determined by units of lipase activity (Layer and... [Pg.278]

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. [Pg.211]

Pancreatin Obtained from porcine or bovine (ox) pancreatic tissue. Produced as a white to tan, water-soluble powder. Major active principles (1) a-amylase, (2) protease, and (3) lipase. Typical applications used in the preparation of precooked cereals, infant foods, and protein hydrolysates. [Pg.147]

Application and Principle These procedures are used to determine the primary enzyme activities in pancreatin preparations. [Pg.917]

Standard Preparation Weigh accurately about 20 mg of USP Pancreatin Reference Standard into a suitable mortar. Add about 30 mL of pH 6.8 Phosphate Buffer, and triturate for 5 to 10 min. Transfer the mixture with the aid of pH 6.8 Phosphate Buffer to a 50-mL volumetric flask, dilute with pH 6.8 Phosphate Buffer to volume, and mix. Calculate the activity, in USP Units of amylase activity per mL, of the resulting solution from the declared potency on the label of the Reference Standard. [Pg.918]

Assay Preparation For Pancreatin having about the same amylase activity as the USP Pancreatin Reference Standard, weigh accurately about 40 mg of Pancreatin into a suitable mortar. [Pg.918]

Note For Pancreatin having a different amylase activity, weigh accurately the amount necessary to obtain an Assay Preparation having amylase activity per mL corresponding approximately to that of the Standard Preparation. [Pg.918]

Standard Test Dilution Suspend about 200 mg of USP Pancreatin Reference Standard, accurately weighed, in about 3 mL of cold water in a mortar, triturate for 10 min, and add cold water to a volume necessary to produce a concentration of 8 to 16 USP Units of lipase activity per mL, based on the declared potency on the label of the Reference Standard. Maintain the suspension at 4°, and mix before using. For each determination, withdraw 5 to 10 mL of the cold suspension, and allow the temperature to rise to 200 before pipeting the exact volume. [Pg.918]

Calculation From the Standard Test Dilution, plot the volume of 0.1 A sodium hydroxide titrated against time. Using only the points that fall on the straight-line segment of the curve, calculate the mean acidity released per min by the Assay Test Dilution. Taking into consideration dilution factors, calculate the lipase activity of the Standard Test Dilution, using the lipase activity of the USP Pancreatin Reference Standard stated on the label. [Pg.919]

Assay Test Dilution Add about 100 mg of USP Pancreatin Reference Standard, accurately weighed, to 100.0 mL of Buffer Solution, and mix by shaking intermittently at room temperature for 25 min. Dilute quantitatively with Buffer Solution to obtain a dilution that corresponds in activity to the Standard Test Dilution. [Pg.919]

Calculation Correct the absorbance values for the filtrates from tubes Si, S2, and S3 by subtracting the absorbance values for the filtrates from tubes SiB, S2B, and S3B, respectively, and plot the corrected absorbance values against the corresponding volumes of the Standard Test Dilution used. From the curve, using the corrected absorbance value (U - UB for the USP Pancreatin Reference Standard taken), and taking into consideration the dilution factors, calculate the protease activity, in USP Units, of the USP Pancreatin Reference Standard taken by comparison with that of the standard, using the protease activity stated on the label of USP Pancreatin Reference Standard. [Pg.919]


See other pages where Pancreatin Activity is mentioned: [Pg.152]    [Pg.828]    [Pg.917]    [Pg.22]    [Pg.152]    [Pg.828]    [Pg.917]    [Pg.22]    [Pg.356]    [Pg.295]    [Pg.1506]    [Pg.4]    [Pg.211]    [Pg.329]    [Pg.16]    [Pg.193]    [Pg.180]    [Pg.219]    [Pg.172]    [Pg.918]    [Pg.140]    [Pg.281]   
See also in sourсe #XX -- [ Pg.917 , Pg.918 ]




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Pancreatine

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