Bile acid output and the interdigestive migrating motor complex in normals and in cholecystectomy patients.

Bile acid output in the duodenum was studied in relation to the interdigestive migrating motor complex in normal subjects and in cholecystectomy patients. In normal volunteers the bile acid output preceding a duodenal activity front (217 +/- 89 mumol/30 min) was 374% of the output following a front (58 +/- 24 mumol/30 min) (P < 0.05).

Motilin and the interdigestive migrating motor complex in man.

In order to assess the possible role of the new candidate gut hormone, motilin, in controlling the interdigestive migrating motor complex (MMC) in man, 14 normal subjects were studied after an overnight fast by means of three pressure-recording catheters with orifices 25 cm apart in the upper small intestine. The typical aboral progressing bursts of pressure waves occurred at a mean interval of 137 minutes and were preceded by a peak motilin level 25 pmol/liter higher than the lowest level in the postactivity-front quiescent period. To study the effect of exogenous motilin, an infusion of pure porcine motilin at various dose levels was given to 16 normal volunteers shortly after the onset of the phase I quiescent period.

The secretory component of the interdigestive migrating motor complex in man.

Intraduodenal pH, bicarbonate and amylase secretion, and gastric acid and pepsin output were studied in relation to the migrating motor complex in man. The occurrence of a motor complex in the duodenum was preceded by an increase in gastric acid and pepsin output and followed by a peak in bicarbonate and amylase secretion. It is concluded that the interdigestive phase in man is characterized by periodic activity complexes comprising both motor and secretory components.

Role of gastrin and insulin in postprandial disruption of migrating complex in dogs.

The duration of the disruption of the interdigestive migrating myoelectric complex (MMC) by various test meals in dogs was correlated with changes in serum gastrin and insulin levels. The test meals consisted of milk protein, sucrose, arachis oil and medium chain triglycerides (MCT). Intravenous infusions of glucose 20% were also used.

Radioimmunoassay for urinary lysozyme in human serum from leukemic patients.

We present a radioimmunoassay for lysozyme in human serum, based upon human lysozyme isolated from the urine of leukemic patients and antiserum prepared against this lysozyme in the goat. In the separation step, a second antibody is used. By properly adjusting the concentrations of unlabeled and 125I-labeled lysozyme and of the antibodies, maximal precision (SD, 0.

Evaluation of the discriminative power of lipidophoresis by discriminant analysis using a simple quantitative method of agarose lipidophoresis.

A simple, reproducible and quantitative method for separation of lipoproteins in agarose is presented. The validity of the results is shown by comparison with gravimetric analysis of fractions separated by ultracentrifugation in a discontinuous NaCl-KBr gradient. Results for a large group of normals and of patients with various lipid disorders are presented, and discriminant analysis is used to evaluate objectively the potential of lipidophoresis in the classification of hyperlipoproteinemias.

Choice of monitoring isotope in double label radioimmunoassays with nonimmunological separation techniques.

We discuss the suitability of some radioactive isotopes as volume markers in radioimmunoassays, from a radiochemical point of view. For three eligible isotopes (22Na, 60Co, and 75Se) we studied the concentration of the marker in the precipitate formed in the separation phase of radioimmunoassays. For all those kinds of separations tested (charcoal, ammonium sulfate, polyethylene glycol, and ethanol), binding or coprecipitation was virtually absent or negligible with 22Na but 75Se was strongly concentrated in the precipitate.

Factors influencing lysozyme determinations by the lysoplate method.

Some factors influencing the lysoplate method have been investigated. The influences of pH, ionic strength and temperature of the gel medium can be explained by considering the influence of these factors upon the diffusion rate rather than upon the enzymatic properties of lysozyme. Salts and proteins present in a sample probably affect the results in a similar way.

Purification and partial characterization of lysozyme from mouse small intestine.

Lysozyme was isolated from the small intestine of mice by combined ion-exchange and molecular sieve chromatography. This lysozyme differs from that isolated from the urine of mice with monocytoma in amino acid composition, and migration rate in cellulose acetate electrophoresis. As intestinal lysozyme originates at least in part from the Paneth cell, our results point towards the existence of isozymes of lysozymes in mice.

The inhibition of lysozyme by bile acids.

The effect of bile acids on the bacteriolytic activity of lysozyme towards Micrococcus lysodeikticus was studied in vitro. All bile acids tested inhibited lysozyme activity. Conjugated bile acids were better inhibitors than their unconjugated homologs and sulfation resulted in still stronger inhibition.

Serum lysozyme levels in Crohn's disease and ulcerative colitis.

Serum lysozyme levels were determined in healthy volunteers, patients with Crohn's disease, and patients with ulcerative colitis. The mean concentration in Crohn's disease was significantly greater than in the other groups. In patients with Crohn's disease, as well as in patients with ulcerative colitis, the lysozyme levels correlated with the severity of the disease process and with the extent of the lesions: the more severe the disease and the more extensive the involvement, the higher the lysozyme levels.

The Paneth cell: a source of intestinal lysozyme.

An antiserum prepared against lysozyme isolated from mucosal scrapings of mouse small intestine was used to stain sections of mouse small intestine with the indirect fluorescent antibody technique. Mucosal fluorescence was confined to the base of the crypts of Lieberkuhn, where Paneth cells are located. After the intravenous administration of 4 mg of pilocarpine fluorescence was no longer found in the Paneth cell but in the crypt lumen.