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H E Seppä

Publications and source records attributed to H E Seppä.

4 recordsLinked to original sources
PubMed1979

The main neutral protease of rat skin is a mast cell enzyme. Immunohistochemical localization of the enzyme in rat skin with the peroxidase-antiperoxidase (PAP) complex method.

The highly sensitive PAP immunoperoxidase method was used to localize the main neutral protease of rat skin. The use of the neutral detergent, Triton X-100, in the reagent and washing solutions was observed to effectively decrease the nonspecific staining. The specific staining was localized to the mast cell granules.

Animals↗
PubMed1978

Rat skin main neutral protease: immunohistochemical localization.

Specific antiserum against the purified rat skin main neutral protease was used in double layer immunofluorescent method to localize the enzyme in normal rat skin. The specific immunofluorescence was seen in dermal cells that were identified as mast cells on basis of their metachromatic granules. Enzyme histochemical staining with naphthol AS-D chloroacetate localized to the same cells that exhibited specific immunofluorescence. The granules of isolated rat mast cells also gave a specific reaction with the immunohistochemical technique. The results provide further evidence for the suggestion that rat skin main neutral protease is identical with the rat mast cell "chymase."

Animals↗
PubMed1976

A rat skin acid esteroprotease hydrolyzing benzoylarginine ethylester: purification and properties.

A benzoylarginine ethylester hydrolyzing enzyme from rat skin has been purified 54-fold by chromatography on arginine methylester-CH-Sepharose and Sephadex G-200 prior to isoelectrofocusing. The molecular weight of the enzyme is approximately 125,000. The enzyme hydrolyzes bensoylarginine ethylester, acetyltyrosine ethylester, benzoylarginine methylester, benzoyllysine methylester, and benzoylalanine methylester. Casein is slightly hydrolyzed at an optimum pH of 6.5. The enzyme is inhibited by diisopropylfluorophosphate, and p-chloromercuribenzoic acid. KC1 enhances the extraction of the enzyme, increased its activity, and is essential for its stability.

Animals↗