Protein Composition and Biogenesis of the Pancreatic Zymogen Granules

Localization of amylase,chymotrypsinogen and trypsinogen in pancreas was demonstrated by Yasuda and Coons (1966), by using fluorescent antibody method. These enzymes were naturally found in the zymogen granules. Among them, amylase showed a diffuse localization around the nucleus, in addition to the zymogen granules. Using ferritin antibody method, scattered ferritin granules were also found around the Golgi area (Yasuda et al.,1967). The recent advance in the tissue preparation enables the antigen to be localized in the ultrathin frozen sections, by applying the labeled antibodies onto the sections instead of staining the tissue en bloc.The present study deals with the comparison of the localization of amylase and lipase demonstrated by applying the bismuth-labeled, peroxidase-labeled and ferritin-labeled antibody methods on the ultrathin frozen sections of pancreas, and on the blocks of the same tissue.

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A complex network of “snake-like tubules” revealed by the NADPase cytochemical reaction in the acinar cell of pancreas

Proceedings, annual meeting, Electron Microscopy Society of America ◽

10.1017/s0424820100113214 ◽

1984 ◽

Vol 42 ◽

pp. 666-667

Author(s):

A.R. Beaudoin ◽

G. Grondin ◽

A. Lord ◽

M. Pelletier

Keyword(s):

Acinar Cell ◽

Lead Acetate ◽

Ultrastructural Localization ◽

Sodium Acetate Buffer ◽

Zymogen Granules ◽

Sprague Dawley ◽

Dense Bodies ◽

Sprague Dawley Rats ◽

Cytochemical Reaction ◽

Cellular Organelles

We have recently described the ultrastructural localization of NADPase activity in the exocrine pancreas of rat. The enzyme was found in the intermediate saccules of the Golgi apparatus, in dense bodies and lysosomes but was absent from zymogen granules. A very intense reaction was noticed in a peculiar structure which was termed “Snake-Like Tubule” (SLT). The purposes of the present study were firstly to delineate SLT distribution in the acinar cell and secondly to define any possible relationship or association with other cellular organelles.NADPase cytochemical reaction was performed on the pancreas of adult Sprague Dawley rats. Small lobules were excised and fixed for 50 min, at 4°C, in 2% glutaraldehyde buffered with 0.1M cacodylate at pH 7.2. Lobules were rinsed several times with the same buffer containing 570 sucrose and cut with a Mcllwayn tissue chopper. Sections were washed several times with buffer and incubated for 2 hr at 37°C in the following medium: 4mM NADPH; 40mM sodium acetate buffer, pH 5.0; 4mM lead acetate and 5% sucrose.

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Bovine Platelet Proteins

Thrombosis and Haemostasis ◽

10.1055/s-0038-1653555 ◽

1969 ◽

Vol 21 (03) ◽

pp. 409-418 ◽

Cited By ~ 2

Author(s):

S Łopaciuk ◽

N. O Solum

Keyword(s):

Bovine Serum ◽

Protein Composition ◽

Disc Electrophoresis ◽

Plasma Fibrinogen ◽

Plasma Albumin ◽

Precipitin Line ◽

Bovine Plasma ◽

Platelet Proteins

Summary1. The protein composition of bovine platelet extracts has been investigated by immunoelectrophoresis and polyacrylamide disc electrophoresis. The information obtained is discussed as a basis for study on platelet fibrinogen.2. With antiserum to platelet proteins 11 precipitin lines were observed 3 of which corresponded electrophoretically to plasma albumin, fibrinogen and γ-globulin. These lines were not seen using the same antiserum absorbed with bovine plasma. The 8 additional lines were still present indicating that they represented specific platelet components. Antiserum to plasma produced the 3 above-mentioned lines, but no others.3. With antiserum to purified bovine plasma fibrinogen 3 precipitin lines were observed. The fibrinogen line was the dominant one. The 2 additional lines did not disappear by absorption of the antiserum with bovine serum nor by incubation of the extracts with thrombin. The latter treatment totally removed the fibrinogen line.4. A non-fibrinogen precipitin line, observed only with the antiserum to platelet extract and positioned in the β2-globulin region, disappeared by the incubation of platelet extracts with thrombin.

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