The Effect of Duodenal Juice on the Intrinsic Factor (IF) Activity in Gastric Juice

SummaryGastric juice from 15 normals, 20 patients with gastric ulcer and 4 patients with erosive haemorrhagic gastroduodenitis was investigated in respect of its activity on unheated and heated fibrin plates and its content of FDP and plasminogen or plasmin with immunochemical methods. Gastric juice from normals showed no activity on unheated and heated fibrin plates, and no FDP or plasminogen could be demonstrated. In the patients with gastric ulcer the gastric juice showed little or no fibrinolytic activity on fibrin plates except in 2, who had regurgitation of duodenal juice and neutral pH of the juice. These patients had equally high activity on heated as on unheated plates and no plasmin could be demonstrated. It was shown that this activity was not due to fibrinolysis, but to non-specific proteolytic activity (probably trypsin). The patients with erosive haemorrhagic gastroduodenitis exhibited quite a different picture. The gastric juice from these patients showed extremely high activity on fibrin plates, the activity was higher on unheated than on heated plates. The activity was inhibited in vitro by addition of EACA and in vivo after administration of AMCA. The occurrence of plasmin could be demonstrated directly immunologically in the gastric juice. By comparison of plasmin and trypsin in various assays it could further be proved that the gastric juice in these cases contained plasminogen activator and plasmin. The patients with erosive haemorrhagic gastroduodenitis showed no increase in fibrinolysis in the blood, but low values for plasminogen and α2M, and the serum contained FDP. These findings in the blood and gastric juice were interpreted as signs of local fibrinolysis in the stomach and duodenum. There is reason to assume that this gastric fibrinolysis contributes substantially to the bleeding tendency. The effect of administration of AMCA on fibrinolytic activity and the haemorrhage lends support to the assumption of such a mechanism.

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Rapid Charcoal Assay for Intrinsic Factor (IF), Gastric Juice Unsaturated B12 Binding Capacity, Antibody to IF, and Serum Unsaturated B12 Binding Capacity

Blood ◽

10.1182/blood.v25.6.875.875 ◽

1965 ◽

Vol 25 (6) ◽

pp. 875-884 ◽

Cited By ~ 481

Author(s):

CHESTER GOTTLIEB ◽

KAM-SENG LAU ◽

LOUIS R. WASSERMAN ◽

VICTOR HERBERT

Keyword(s):

Small Molecules ◽

Gastric Juice ◽

Rapid Method ◽

Molecular Sieve ◽

Clinical Laboratory ◽

Binding Capacity ◽

Intrinsic Factor ◽

Wide Range ◽

Charcoal Particle ◽

Ready Availability

Abstract The principle of the dialysis assays for intrinsic factor (IF) and antibody to IF was integrated with the demonstration that protein-coated charcoal adsorbs only free and not bound B12, in a single rapid method for 4 separate assays: (1) assay of IF, (2) assay of gastric juice unsaturated B12 binding capacity, (3) assay of serum antibodies to IF and (4) assay of serum unsaturated B12 binding capacity. The method is sensitive, accurate, reproducible, and can easily be completed within an hour. The simplicity and ready availability of reagents and equipment lends itself to ready adoption in any clinical laboratory using radioisotopes. The charcoal particle is considered as a solid microsponge, and its coat of albumin, other protein, carbohydrate, or other large molecule as a molecular sieve surrounding the sponge. The whole constitutes a system of "instant dialysis," with a wide range of applications in the separation of large from small molecules.

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On the Nature of Castle’s Hemopoietic Factor

Blood ◽

10.1182/blood.v6.12.1234.1234 ◽

1951 ◽

Vol 6 (12) ◽

pp. 1234-1239 ◽

Cited By ~ 30

Author(s):

SHEILA T. CALLENDER ◽

L. G. LAJTHA

Keyword(s):

Vitamin B12 ◽

Gastric Juice ◽

Intrinsic Factor ◽

Normal Serum ◽

Relationship Of ◽

The Relationship

Abstract 1. Normal gastric juice (intrinsic factor) and vitamin B12 together form a thermolabile hemopoietic factor which ripens megaloblasts in vitro, both gastric juice and B12 alone being inactive. 2. The hemopoietic factor in normal serum which ripens megaloblasts in vitro also appears to be thermolabile, heating to 56 C. for 2 hours destroying some of its activity. 3. The relationship of these factors is discussed and an extra-gastric as well as a gastric source of intrinsic factor is postulated.

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Evidence that Pancreatic Proteases Enhance Vitamin B12 Absorption by Acting on Crude Preparations of Hog Gastric Intrinsic Factor and Human Gastric Juice

Gastroenterology ◽

10.1016/s0016-5085(77)80299-0 ◽

1977 ◽

Vol 72 (1) ◽

pp. 31-36 ◽

Cited By ~ 12

Author(s):

Phillip P. Toskes ◽

George W. Smith ◽

Gary M. Francis ◽

Eugene G. Sander

Keyword(s):

Vitamin B12 ◽

Gastric Juice ◽

Intrinsic Factor ◽

Human Gastric Juice ◽

Pancreatic Proteases ◽

Vitamin B12 Absorption

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Inhibition of Free Intrinsic Factor Activity by Duodenal Juice

Gastroenterology ◽

10.1016/s0016-5085(19)33900-9 ◽

1969 ◽

Vol 57 (3) ◽

pp. 273-279 ◽

Cited By ~ 4

Author(s):

I.J. Temperley ◽

D.G. Weir ◽

D. Collery ◽

J.M. Scott

Keyword(s):

Intrinsic Factor ◽

Duodenal Juice ◽

Factor Activity

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Functional activity of intrinsic factor measured by using solubilized receptor protein.

Clinical Chemistry ◽

10.1093/clinchem/28.8.1794 ◽

1982 ◽

Vol 28 (8) ◽

pp. 1794-1796 ◽

Cited By ~ 1

Author(s):

G Marcoullis ◽

S P Rothenberg

Keyword(s):

Gastric Juice ◽

No Value ◽

Functional Activity ◽

Sodium Sulfate ◽

Intrinsic Factor ◽

Receptor Site ◽

Final Concentration ◽

Receptor Protein ◽

Species Specific ◽

Protein Reagent

Abstract The traditional radioimmunoassay for gastric intrinsic factor, in which this protein is measured on the basis of immunoreactivity rather than function, is of no value for identifying intrinsic factor that binds cobalamin but does not bind to the ileal receptor site, or for detecting animal intrinsic factor, which does not cross react with human intrinsic factor. Accordingly, we have applied a radioassay for the intrinsic factor receptor protein to measure the functional activity of intrinsic factor in gastric juice. The receptor protein reagent was partly purified from guniea pig ilea and its interaction with intrinsic factor--CN[57Co]-cobalamin was determined by precipitation with sodium sulfate at a final concentration of 150 g/L. Results of this assay were comparable with results obtained for intrinsic factor by radioimmunoassay. The receptor protein did not bind immunoreactive intrinsic factor that was functionally abnormal. This functional radioassay for intrinsic factor is not species specific and will be of value when specific antiserum to intrinsic factor is not available and when cobalamin malabsorption is to be evaluated in patients who are secreting normal amounts of immunoreactive intrinsic factor.

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