Role of the autonomic nervous system in the release of rat submandibular gland kallikrein into the circulation.

We have previously demonstrated that the rat submandibular gland releases immunoreactive kallikrein into the circulation. To study the role of the autonomic nervous system in this release, submandibular gland blood flow and kallikrein concentration in peripheral arterial and venous blood from the gland were measured and secretion rates calculated before and after parasympathetic and sympathetic nerve stimulation (8V, 2 msec, 10 Hz) for 1 minute. Immunoreactive kallikrein in plasma was measured by radioimmunoassay, and timed collections of venous outflow were used to measure blood flow.

Excess antibody immunoassays for rat glandular kallikreins. Measurement of kallikrein from different organs in the presence of cross-reacting antigens.

An immunoradiometric assay has previously been developed for measurement of rat glandular kallikrein. In the present paper, further studies on the specificity and sensitivity of the method are described. Problems of interference of immunologically cross-reacting antigens were overcome by proper preabsorption of the antibody.

Excess antibody immunoassay for rat glandular kallikrein. Monosized polymer particles as the preferred solid phase material.

The development of an excess antibody assay for rat glandular kallikrein is described. This assay permits immunological determination of kallikrein as well as a simultaneous specific measurement of kallikrein enzymatic activity. The assay is based on coupling of immunopurified anti-kallikrein immunoglobulin to a solid phase.

A 4-methoxy-2-naphthylamide substrate for the histochemical localization of esteroproteases in the submandibular gland of the rat.

The 4-methoxynaphthylamide (MNA) derivative of D-Val-Leu-Arg-4-MNA has been used as a substrate for the histochemical localization of esteroproteases in the submandibular gland of rats, and compared with the substrate alpha N-O-met. The hydrolysis of Val-Leu-Arg-4-MNA by esteroproteases was investigated using spectrophotometry and isoelectric focusing. Both methods demonstrated that the substrate is cleaved by different enzymes and is not a monospecific kallikrein marker, although Val-Leu-Arg-4-MNA had a much smaller spectrum of enzyme activities than alpha N-O-met.