Swine Pancreas Research Articles

Plasma lipase properties as related to pancreatic condition.

We examined the sensitivity to colipase of two types of lipase (EC 3.1.1.3) activity in plasma. Results were very similar for plasma lipase corresponding to that found in cases of acute pancreatitis and for swine pancreas lipase, whereas we found some differences between "pancreatitis lipase" and lipase from healthy subjects. Gel-filtration experiments suggest that the two forms of lipase in plasma have different relative molecular masses; moreover, their avidity for antibodies against human pancreatic lipase differs. Guided by these studies, we propose optimal conditions for nephelometry of "pancreatitis" lipase.

4393140 Process for the preparation of the highly pure enzyme kallikrein from swine pancreas extracts: Hermann Schutt, Wuppertal, Federal Republic of Germany assigned to Bayer Aktiengesel-lschaft

4393140 Process for the preparation of the highly pure enzyme kallikrein from swine pancreas extracts: Hermann Schutt, Wuppertal, Federal Republic of Germany assigned to Bayer Aktiengesel-lschaft

Hydrolysis of an aliphatic monoester in emulsion by swine pancreas lipase: influence of interfacial bile salts molecules upon reaction rate

The accumulation of four bile salts at the interface between water and n-hexyl laurate is studied. Gibb's interfacial excesses of these salts are calculated, starting from interfacial tension measurements. At the same time, emulsions of the ester are treated by lipase and reactions rates are plotted against the bile salt concentrations present in the water phase of the emulsions. Inhibition by conjugated bile salts appear before the critical micellar concentration is approached. There is no defined relationship between this inhibition and the fraction of interfacial area covered by detergent molecules. In accordance with recent publication, the discussion suggests that the energy level of interfaces is important for lipase action and that, when interfacial tension becomes too small, lipase does not attach to interfaces and appears as inactive.

X-ray crystallographic analysis of swine pancreas α-amylase

α-Amylase has been purified from swine pancreas by adsorption onto glycogen and crystallized from concentrated protein solutions in the presence of Ca 2+. Two morphological forms have been obtained and X-ray analysis has shown them both to be of space group P2 12 12 1 with a = 70 A ̊ , b = 110 A ̊ and c = 117 A ̊ . There are two molecules of total molecular weight 90 000 in the asymmetric unit. The diffraction pattern extends to a resolution of better than 3 Å and appears to be stable to radiation exposure.

Histological and histochemical studies of the islands of Langerhans of the swine pancreas (Sus scrofa)

Histological and histochemical studies of the islands of Langerhans of the swine pancreas (Sus scrofa)

Isolation and partial characterization of an elastase-associated acidic endopeptidase and its interaction with elastase at low ionic strength

An acidic endopeptidase has been isolated from dried preparations of swine pancrease by column chromatography on DEAE cellulose. The yield of acidic endopeptidase from 100 g of pancreas powder was 210 mg. The product was found to be electrophoretically homogeneous and produced a single peak in the analytical ultracentrifuge. The sedimentation coefficient (s 0 20,w) , diffusion coefficient (D 20,w) , apparent molecular weight, electrophoretic mobility, E 1 cm 1% at 280 mμ and pH optimum were respectively, 3.13, 8.7 · 10 −7 cm 2 · sec −1 , 35 300, −5.9 · 10 −5 cm 2 · V −1 · sec −1 , 14.6 and 10.7. The enzyme was inhibited by diisopropyl phosphorofluoridate, by swine serum and to a lesser extent by human serum. It was not “activated” by 1 · 10 −3 M FeCl 2 , MnCl 2, MgCl 2, CaCl 2 or CoCl 2 or by 1 · 10 −3 M ZnSO 4 ; however, the activity of the enzyme was increased by 1 · 10 −3 M cysteine. The similarity of the acidic endopeptidase to proteolytic enzymes described by other investigators is discussed. Gradient elution ion-exchange chromatography of water insoluble elastase euglobulin produces two major water soluble components, elastase and the acidic endopeptidase. When distilled water solutions of the purified enzymes were mixed complex formation occurred (precipitation) between the basic protein elastase and the acidic endopeptidase. The formation of the euglobulin when acid extracts of swine pancreas are dialyzed against distilled water is thus explained. Complex formation was maximal at low ionic strength when the enzymes were oppositely charged and was minimal below the isoelectric point of the acidic endopeptidase (∼ pH 4.1) or above the isoelectric point of elastase (pH 9.5). The reaction was essentially abolished at I 0.011. The equivalence point for the reaction was 2.8 mg of elastase  1 mg of acidic endopeptidase. One mole of acidic endopeptidase is capable of binding approximately four moles of elastase. Although trypsin, another basic protein, was precipitated by the acidic endopeptidase the data suggest a preferential reaction of the latter enzyme with elastase.