Literature DB >> 173439

Granule enzymes of polymorphonuclear neutrophils: A phylogenetic comparison.

P G Rausch, T G Moore.   

Abstract

The functional significance of granule enzymes in polymorphonuclear leukocytes (PMN) is not fully understood because of the multiplicity of the enzymes and the rare occurrence of deficiencies in man. In order to select appropriate laboratory animals for functional studies, a phylogenetic comparison of enzyme levels in animal and human PMN was undertaken. Neutrophils were obtained from a variety of laboratory animals and man; the activities of alkaline phosphatase, lysozyme, myeloperoxidase, and beta-glucuronidase were determined by histochemical and analytical techniques. Marked interspecies differences in enzyme activity were found; many species were deficient in alkaline phosphatase or lysozyme. Differences in pH optima and metal requirements of alkaline phosphatase were not of sufficient magnitude to explain the variations of this enzyme.

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Year:  1975        PMID: 173439

Source DB:  PubMed          Journal:  Blood        ISSN: 0006-4971            Impact factor:   22.113


  46 in total

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Review 5.  Mouse versus Human Neutrophils in Cancer: A Major Knowledge Gap.

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Journal:  Trends Cancer       Date:  2017-01-19

Review 6.  Myeloperoxidase in human neutrophil host defence.

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7.  Evaluation of oxygen-dependent immunodefences of the polymorphonuclear cells of some tropical ruminants.

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Review 8.  Myeloperoxidase: a front-line defender against phagocytosed microorganisms.

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9.  Neutropenia in cats with the Chediak-Higashi syndrome.

Authors:  D J Prieur; L L Collier
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10.  Effect of N-acetylcysteine on the pulmonary response to endotoxin in the awake sheep and upon in vitro granulocyte function.

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