Isozyme Variations in Human Cells Grown &lt;i&gt;in vitro&lt;/i&gt;. VII. Subcellular Distribution of Ammo Acid Naphthylamidases

Lundgren, Ewa

doi:10.1159/000152453

Cited by 10 publications

(3 citation statements)

References 6 publications

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“…The results indicated that the activities against the different sub strates were inhibited to different degrees (table III). If the enzyme requiring the presence of Triton X-100 to be extracted is similarly affected, a point that we are not certain about (21), then the relative amount of enzyme in our Triton X-100 extracts would be 40-60% higher than our figures indicate. teoglycans, and a lower molecular weight frac tion (~ 230,000 daltons).…”

Section: Effect Of Triton X-100 On the Extraction Of Naphthylamidasesmentioning

confidence: 56%

Naphthylamidase (Arylaminopeptidase) Activities in Rat Cartilages and Bone

Hirschman¹,

Hirschman²

1977

Enzyme

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Extracts of epiphyseal articular and costal cartilages and of metaphyseal bone showed different profiles of activity against 21 aminoacyl β-naphthylamides. Except for the activity against arginyl and lysyl j3-naphthylamides, most of the activities required the presence of Triton X-100 for extraction, suggesting that in situ, the enzymes are bound to or within membranous structures. Histochemical studies demonstrated that most, if not all, activity was intracellular. The activity is enhanced by Co^2+. TAME (2 X 10^-4 mol/1) inhibits activity against leucyl β-naphthylamide and some others, but has little, if any, inhibition of activity against alanyl β-naphthylamide. Gel filtration of the extract showed a high molecular weight active fraction eluting with proteoglycan, and an active fraction with an approximate molecular weight of about 230,000. Two active fractions are obtained by gradient elution from DEAE-cellulose.

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Section: Effect Of Triton X-100 On the Extraction Of Naphthylamidasesmentioning

confidence: 56%

Naphthylamidase (Arylaminopeptidase) Activities in Rat Cartilages and Bone

Hirschman¹,

Hirschman²

1977

Enzyme

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“…Beckman/L undgren/T arnvik The subcellular localization of the A and B isozymes in the KB cell line was studied by means of differential centrifugation according to the method described by Lundgren [1971b]. The fractions were made equal with respect to the protein concentration and examined by means of starch gel electrophoresis and subsequent staining for superoxide dismutase.…”

mentioning

confidence: 99%

Superoxide Dismutase Isozymes in Different Human Tissues, Their Genetic Control and Intracellular Localization

1973

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Two isozymes of superoxide dismutase, A and B, were found in extracts of human organs, tissues and cell cultures. Differential centrifugation of cell homogenates revealed that isozyme A was localized in the soluble phase and isozyme B in fractions enriched in mitochondria. Isozyme B was lacking in erythrocytes and isozyme A in polymorphonuclear leucocytes. All other specimens showed both isozymes although in variable proportions. Evidence was presented suggesting that isozymes A and B are controlled by genes at separate gene loci. The occurrence of hybrid enzyme in a heterozygous phenotype of isozyme A suggests that the isozyme is a dimer made up of two identical polypeptide subunits.

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“…Another possibility is that a microsomal organelle has this density. Acid phosphatase and amino acid naphthylamidase have been demonstrated in cultured HeLa cells in a mirrosomal fraction (Lundgren 1971 ) .…”

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confidence: 99%

Enzymatic Heterogeneity of Granules in Human Leucocytes

Lundgren

Roos

Tärnvik

1975

Acta Pathologica Microbiologica Scandinavica Section A Patholog

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Homogenates of highly purified polymorphonuclear leucocytes and of a mixture of mononuclear leucocytes and platelets from human blood were separated by differential and isopyknic centrifugation. A heterogeneity in granules containing digesting enzymes was found in both cell preparations. Enzymes typical of lysosomes were found in the two cell preparations in a similar density range. Granules of low density were indicated in polymorphonuclear leucocytes by alkaline phosphatase. In both cell preparations a third granule, of lower density, seemed to exist enriched in amino acid naphthylamidase, acid hydrolases and in polymorphonuclear leucocytes also alkaline phosphatase and lysozyme. A remarkable difference between the two cell preparations was the occurrence of amino acid napthylamidase in denser granules of polymorphonuclear leucocytes only, although the nature of these granules could not be determined.

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Isozyme Variations in Human Cells Grown <i>in vitro</i>. VII. Subcellular Distribution of Ammo Acid Naphthylamidases

Cited by 10 publications

References 6 publications

Naphthylamidase (Arylaminopeptidase) Activities in Rat Cartilages and Bone

Naphthylamidase (Arylaminopeptidase) Activities in Rat Cartilages and Bone

Superoxide Dismutase Isozymes in Different Human Tissues, Their Genetic Control and Intracellular Localization

Enzymatic Heterogeneity of Granules in Human Leucocytes

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