Pig pancreas

Fischer, brilliant results were achieved, and in succession the a-amylases of pig pancreas, of Bacillus subtilis, of human saliva, of human pancreas, and of Aspergillus oryzae, and the /3-amylase of malt, were successfully crystallized. Important biological deductions were gained from this study whereas the amylases of human pancreas and saliva cannot be distinguished from one another, amylases from pig pancreas and from human pancreas are different. These differences are manifested in molecular weight, crystalline forms, electrophoretic mobility, and influence of the pH on the activity however, all the amylases have the same specific biochemical action. The identity of the enzymes seems to be dependent on the species and not on the organ. Interest in biologically active proteins led Meyer to a study of the protein hormones, a field in which he was very active at the time of his death. 

Eng J, Kleinman WA, Singh L, Singh G Raufman JP. (1992) Isolation and characterization of exendin-4, an exendin-3 analogue, from Heloderma sus-pectum venom. Further evidence for an exendin receptor on dispersed acini from guinea pig pancreas. J Biol Chem 267 7402-7405. 

R) -glycidyl butanoate (RS) -glycidyl butanoate pig pancreas lipase... 

Source of Enzyme (s) Pig pancreas A. sclerotiorum S. cerevisiae Rhodococcus rhodochrous Achromobacter xylosooxydans... 

Lipases (triacyl glycerol acyl hydrolases, E.C 3.1.1.3) are a unique class of hydrolases for asymmetric synthesis86,87,S9,90e, They are available from fungi, bacteria and mammalians. The lipases most commonly used so far are the commercially supplied pig pancreas lipase (PPL)136, Pseudomonas cepacia lipase (PCL)89,137 and Candida cylindracea lipase (CCL). In most cases only the crude lipases, consisting of a mixture of proteins which may even be other hydrolases, are successfully applied1373. 

Other microbial lipases have also been successfully used in anhydrous ionic liquids, e.g., from Alcaligenes sp. (AsL) [54, 58], CaLA, Rhizomucor miehei lipase (RmL), and Thermomyces lanuginosus lipase (TIL) [54]. The lipase from pig pancreas (porcine pancreas lipase, PPL), the only mammalian lipase that has been subjected to ionic liquids, catalyzed transesterificationin[BMIm][NTf2]butnotin[BMIm][PF6]... 

Bovine lung or mucous QAE Sephadex A50 Proteases of Bacillus subtilis Proteolytic enzymes from pig pancreas... 

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. 

Submitting this racemic ester to hydrolysis by an enzyme found in pig pancreas leaves enantiomerically enriched ester with the absolute stereochemistry shown. What are the advantages and disadvantages of this method Why is the ee not 100% ... 

Momordica MCE1-1 Momordica charanUa (bitter ELA (pig pancreas) [300nM ... 

From the variation of with temperature (when Michaelis conditions hold), the heat and entropy of formation of the enzyme — substrate complex can be found. Such calculations have been made for the alpha-amylase from pig pancreas, and the alpha- and beta-amylases from malted sorghum. ... 

Enantiomerically pure derivatives of glycerol can be prepared in large quantities through the lipase (pig pancreas EC 3.1.1.3)-catalyzed hydrolysis of prochiral diacetate 28. The procedure gives (R)-29 (45% yield, 88% ee), which can be converted into the crystalline derivatives (7 )-30 or (5 )-30 (>99% ee) as shown in Scheme 13.21 [54]. 

In order to increase the chemical stability of ATP derivatives that possess long thioether tethers, the 1-thiotriphosphate analogues (86) have been prepared from 2-thio-adenosine. These compounds were fourfold more stable to pig pancreas type I ATPDase than ATP. They were also more potent than ATP at stimulating intracellular response and were established as new insulin secreta-... 

Liu H-P, Tay SS-W, Leong S-K (1997b) Localization of glutamate receptor subunits of the a-amino-3-hydroxy-5-methyl-4-isoxazolepropionate (AMPA) type in the pancreas of newborn guinea pigs. Pancreas 74 360-368. 

The application of ionic liquids in lipase biocatalysis has not remained entirely restricted to CaLB, PcL or CrL. Other lipases have been used in ionic liquids for ester synthesis such as Candida antarctica lipase A (CaLA) [15,16], Thermomyces lanuginosus lipase [17] (TLL), Rhizomucor miehei lipase (PmL), Pseudomonas fluorescens lipase (PJL) [18], Pig pancreas lipase (PpL) [17] and Alcaligenes sp. lipase (A5 L) [16]. 

Because of the results with numerous prochiral diesters and diols, which have been subjected successfully to hydrolase-catalyzed enantioselective hydrolysis and acylation, respectively, and because of the desire to predict the sense of the asymmetric induction in the conversion of a new substrate, active-site or substrate models have been developed for the hydrolases pig liver esterase171 731, pig pancreas... 

The lipases most used until now are the commercially supplied pig pancreas lipase (PPL), Pseudomonas cepacia lipase (PCL) or P. Jluorescens lipase (PFL), Candida cylindracea (CCL) or C. rugosa lipase (CRL), Pseudomonas sp. lipase (PSL), increasingly Candida antarctica B lipase (CAL-B) and to a lesser extent further lipases mentioned in Tables 11.1-10 to 11.1-25, and cholesterol esterase (CE). CAL-B is a recombinant protein produced in AspergiUus oryzae accepting a broad range of substrates and conditions. A special group of hydrolases, which are considered as lipases, are the cholesterol esterases (CE), found in mammals and microorganisms1113. ... 

Unsaturation in the alkyl chain frequently leads to the monoacetate of a higher ee value as exemplified with 16 and 17. Comparison of the enantioselectivities of the hydrolysis of diacetates to the corresponding monoacetates is often complicated by the lack of information on the amount of diol formed. The later arises from the hydrolysis of the monoacetate that may proceed under enantiomer differentiation, and thus the ee value of the monoacetate will be a composite of two enantioselective processes. Interestingly, upon changing the configuration of the double bond of the substituent R from ( ) to (Z) the enantiotopic group recognition by pig pancreas lipase inverts, as demonstrated by the monoacetates 8 and 9 as well as 11 and 12 (Table 11.1-10). 

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