Quantitative histochemistry of the nephron. VII. Various phosphatases in the healthy human kidney

Bonting, S.L.; Tsoodle, Alta D.; Bruin, Hendrina de; Mayron, B.R.

doi:10.1016/0003-9861(60)90465-3

Cited by 55 publications

(16 citation statements)

References 19 publications

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“…The lowest levels of LDH activity were found in the glomeruli. This appears to be part of a general pattern emerging from the data reported by McCann for aldolase, fumarase, hexokinase and phosphohexoisomerase in the dog kidney (9), and from our own unpublished results with glucose-6-phosphatase, adenosine triphosphatase and hexokinase (10).…”

Section: Discussionsupporting

confidence: 71%

Quantitative Histochemistry of the Nephron. Iii. Lactic Dehydrogenase Activity in Man and Other Species*

Bonting¹,

Pollak²,

Muehrcke³

et al. 1960

J. Clin. Invest.

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In previous papers (1, 2) we have described observations on the quantitative distribution of alkaline phosphatase in the anatomical units of the nephron in man and other species. This enzyme was selected for study by microdissection of lyophilized sections of kidneys and ultra-microassay because there was considerable information available on its qualitative distribution in the nephron. In particular, the known qualitative differences in its distribution in the proximal and distal convolutions of the tubule allowed us to verify the accuracy of the microdissection technique we used (2). Once this was accomplished we were able to study the quantitative distribution of other enzymes for which less information was available. In this paper the results of assay of lactic dehydrogenase (LDH) activity on renal tissues from healthy humans and laboratory animals are reported. LDH was chosen for study because it plays an important role in energy metabolism, namely, in the glycolytic formation of lactic acid and in its mobilization for complete oxidation in the tricarboxylic acid cycle. As far as could be ascertained, no data were available on its distribution or functional significance in the cells of the nephron.

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Section: Discussionsupporting

confidence: 71%

Quantitative Histochemistry of the Nephron. Iii. Lactic Dehydrogenase Activity in Man and Other Species*

Bonting¹,

Pollak²,

Muehrcke³

et al. 1960

J. Clin. Invest.

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“…In contrast to results previously reported by Bonting et al [6], EDTA at concentrations ranging from 2 X 10~3m to 10.0 X 10~3m failed to show activation of renal acid phosphatase. Instead, inhibitory effects of 3% to 11% were noted.…”

Section: Ionic Strength Effectcontrasting

confidence: 56%

Studies of Human Kidney and Urine Acid Phosphatase

et al. 1970

Enzymol Biol Clin

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The human kidney is a comparatively rich source of the enzyme acid phosphatase; the highest activity is found in the glomeruli. Since glomerular damage might be reflected by excretion of large quantities of this enzyme into the urine, the present study was undertaken to determine the biochemical characteristics of renal acid phosphatase as it appears in human urine and to establish optimum assay conditions for quantitative measurement of urinary enzyme activity. Enzyme kinetics, including substrate concentration requirement, Km values, and incubationtime characteristics, were determined for renal and urinary acid phosphatase. Stability of enzyme activity during storage and the effect of activators and inhibitors of the enzyme were examined. The influence of acid phosphatase activity derived from sources other than the kidney on the measurement of renal enzyme activity in the urine had to be considered; therefore, the selective inhibitory effects of various compounds on acid phosphatase derived from human kidney, prostate, and red and white blood cells have been studied. Renal and prostatic acid phosphatase share similar biochemical features, particularly with regard to selective inhibition. It was not possible to inhibit the urinary acid phosphatase contributed by prostate without simultaneously strongly affecting renal acid phosphatase. On the other hand, a selective inhibition of the urinary acid phosphatase contributed by erythrocytes and partially that contributed by leukocytes could be obtained. Bacteriuria was considered as a further source of error. The results indicate that it may be possible to utilize the measurement of urinary acid phosphatase activity as an index of glomerular damage in children and adult females but not in adult males, because of the contribution of prostatic acid phosphatase.

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“…O f all the enzymes measured in the human kidney to date, only the activity of acid phosphatase [3] and G-6-PDH was found to be higher in the glomeruli than in the other parts of the nephron.…”

Section: Glutaminases G Id H and C A And Their Role In The Productmentioning

confidence: 99%

Quantitative Enzyme Patterns in the Nephron of the Healthy Human Kidney

Mattenheimer¹,

Pollak²,

Muehrcke³

1970

Nephron

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The activity of LDH, MDH, G1DH, GOT, GPT, and CA was measured in the glomeruli, proximal convolutions, distal convolutions, medullary rays, outer zone of the medulla, inner zone of the medulla, and papilla dissected from 16 µ frozen dried sections of the human kidney. The activity of phosphate activated glutaminase, pyruvate activated glutaminase and non-activated glutaminase was determined in fresh homogenates from cortex, medulla and papilla. The enzyme activity was lower in glomeruli than in most other parts of the nephron. The activity of LDH, G1DH, GOT, and CA was highest in the proximal and/or distal convolutions. The maximum MDH and GPT activity was in the medullary rays. The highest activity of the glutaminases was found in cortex, the lowest in the medulla. The distribution patterns in the nephron of CA, glutaminases, GOT, GPT, and G1DH are compatible with the sites found in experimental animals for the production and excretion of hydrogen ion and ammonia, and suggest a very similar localization and mechanism in the human kidney.

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Quantitative histochemistry of the nephron. VII. Various phosphatases in the healthy human kidney

Cited by 55 publications

References 19 publications

Quantitative Histochemistry of the Nephron. Iii. Lactic Dehydrogenase Activity in Man and Other Species*

Quantitative Histochemistry of the Nephron. Iii. Lactic Dehydrogenase Activity in Man and Other Species*

Studies of Human Kidney and Urine Acid Phosphatase

Quantitative Enzyme Patterns in the Nephron of the Healthy Human Kidney

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