scholarly journals Purification of human renin by affinity chromatography using a new peptide inhibitor of renin, H.77 (D-His-Pro-Phe-His-Leu-R-Leu-Val-Tyr)

1983 ◽  
Vol 211 (2) ◽  
pp. 519-522 ◽  
Author(s):  
G D McIntyre ◽  
B Leckie ◽  
A Hallett ◽  
M Szelke
Keyword(s):  
Crude Extract ◽  
Specific Activity ◽  
Human Kidney ◽  
Peptide Inhibitor ◽  
Kidney Cortex ◽  
Affinity Column ◽  
Acid Proteinase ◽  
Human Renin ◽  
Enzyme Specific Activity ◽  
Sepharose 4B

A new affinity column for renin was prepared by coupling the isosteric peptide inhibitor of renin, H.77 (D-His-Pro-Phe-His-LeuR-Leu-Val-Tyr, where R is a reduced isosteric bond, -CH2-NH-), to activated 6-aminohexanoic acid-Sepharose 4B. Chromatography of a crude extract of human kidney cortex on this material resulted in a 5500-fold purification of renin in 76% yield. The purified enzyme (specific activity 871 units/mg) was free of non-specific acid-proteinase activity and was stable at pH 6.8 and −20 degrees C over a period of several weeks.

Purification of Human Renal Renin

1978 ◽  
Vol 55 (s4) ◽  
pp. 117s-119s
Author(s):  
Eve E. Slater ◽  
Robert C. Cohn ◽  
Victor J. Dzau ◽  
Edgar Haber
Keyword(s):  
Enzymatic Activity ◽  
Affinity Chromatography ◽  
Sodium Dodecyl Sulphate ◽  
Gel Electrophoresis ◽  
Specific Activity ◽  
Sodium Dodecyl ◽  
Single Band ◽  
Kidney Cortex ◽  
Human Renin ◽  
Cadaver Kidney

1. Human renal renin has been purified 200 000-fold from cadaver kidney cortex by a method which employs affinity chromatography on aminohexyl pepstatin. 2. The product of this purification has a specific activity of 400 Goldblatt units/mg when compared with Haas human renin standard. 3. This product appears as a single band on sodium dodecyl sulphate gel and polyacrylamide-disc gel electrophoresis. Renin enzymatic activity was recovered after elution from a polyacrylamide-disc gel run at pH 7·8. 4. Yield with this method was 1%.

scholarly journals Thermostable glucose isomerase from psychrotolerant Streptomyces species

1970 ◽  
Vol 1 ◽  
pp. 6-10 ◽  
Author(s):  
Bidur Dhungel ◽  
Manoj Subedi ◽  
Kiran Babu Tiwari ◽  
Upendra Thapa Shrestha ◽  
Subarna Pokhrel ◽  
...  
Keyword(s):  
Specific Activity ◽  
Fold Increase ◽  
Glucose Isomerase ◽  
Enzyme Concentration ◽  
Maximal Velocity ◽  
Ph Optimum ◽  
Streptomyces Spp ◽  
Optimum Ph ◽  
Optimum Reaction ◽  
Sepharose 4B

Glucose isomerase (EC 5.3.1.5) was extracted from Streptomyces spp., isolated from Mt. Everest soil sample, and purified by ammonium sulfate fractionation and Sepharose-4B chromatography. A 7.1 fold increase in specific activity of the purified enzyme over crude was observed. Using glucose as substrate, the Michaelis constant (KM<) and maximal velocity (Vmax) were found to be 0.45M and 0.18U/mg. respectively. The optimum substrate (glucose) concentration, optimum enzyme concentration, optimum pH, optimum temperature, and optimum reaction time were 0.6M, 62.14μg/100μl, 6.9, 70ºC, and 30 minutes, respectively. Optimum concentrations of Mg2+ and Co2+ were 5mM and 0.5mM, respectively. The enzyme was thermostable with half-life 30 minutes at 100ºC.DOI: 10.3126/ijls.v1i0.2300 Int J Life Sci 1 : 6-10

17-Oxidoreduction of 17β-Estradiol, Estrone and Their 3-Sulfates by Kidney Slices from Guinea Pig and Human

1975 ◽  
Vol 53 (12) ◽  
pp. 1333-1336 ◽  
Author(s):  
R. Hobkirk ◽  
Mona Nilsen ◽  
Barbara Jennings
Keyword(s):  
Guinea Pig ◽  
Marked Reduction ◽  
Human Kidney ◽  
Kidney Cortex ◽  
Limited Extent ◽  
Tissue Slices ◽  
Ample Evidence ◽  
Sulfatase Activity ◽  
17Β Estradiol ◽  
Dehydrogenation Reactions

Slices of whole kidney and kidney cortex from the female guinea pig catalyzed a marked reduction of estrone 3-sulfate (E13S) and estrone (E1) to 17β-estradiol 3-sulfate (E23S) and 17β-estradiol (E2), respectively, as well as the reverse (dehydrogenation) reactions. Slices of medulla did not appear active in E23S–E13S interconversion but did possess the ability to interconvert E2 and E1, besides possessing considerable sulfatase activity. The use of [3H-35S]E13S and [3H-35S]E23S as substrates, together with a demonstrated lack of estrogen sulfate synthesis by the tissue slices, provided ample evidence that the intact sulfates were involved in direct oxidoreduction. Slices of human kidney cortex catalyzed the reduction of E13S to a very limited extent. Slices of whole kidney and of cortex from guinea pig formed small amounts of estrogen glucuronide(s).

scholarly journals THE POLARITY OF THE PROXIMAL TUBULE CELL IN RAT KIDNEY

1972 ◽  
Vol 54 (2) ◽  
pp. 232-245 ◽  
Author(s):  
Hans-G Heidrich ◽  
Rolf Kinne ◽  
Eva Kinne-Saffran ◽  
Kurt Hannig
Keyword(s):  
Proximal Tubule ◽  
Plasma Membranes ◽  
Specific Activity ◽  
Rat Kidney ◽  
High Specific Activity ◽  
Kidney Cortex ◽  
Proximal Tubule Cell ◽  
Surface Charges ◽  
Tubule Cell ◽  
Rat Kidney Cortex

Two different membrane fractions were obtained from a brush-border fraction of rat kidney cortex by using their different electrical surface charges in preparative free-flow electrophoresis. One membrane fraction contained only morphologically intact microvilli and was characterized by a high specific activity of alkaline phosphatase. The other fraction morphologically resembled classical plasma membranes by possessing junctional complexes and a high Na-K-ATPase activity The contamination of the isolated membrane fractions by other cell organelles was extremely low These two fractions represent the apical (luminal) and the basal (interstitial) area of the renal proximal tubule cell membrane and clearly demonstrate the polarity of this cell.

scholarly journals Detection of hematopoietic stem cell transcriptome in human fetal kidneys and kidney organoids derived from human induced pluripotent stem cells (iPSC)

2021 ◽  
Author(s):  
Jin Wook Hwang ◽  
Christophe Desterke ◽  
Julien Loisel-Duwattez ◽  
Frank Griscelli ◽  
Annelise Bennaceur-Griscelli ◽  
...  
Keyword(s):  
Stem Cells ◽  
Fetal Liver ◽  
Human Kidney ◽  
Kidney Cortex ◽  
Hematopoietic Stem ◽  
Adult Kidney ◽  
Whole Transcriptome Analysis ◽  
Induced Pluripotent ◽  
Cell Transcriptome ◽  
Kidney Organoids

AbstractBackgroundIn mammalians, hematopoietic stem cells (HSC) arise in the dorsal aorta from the hemogenic endothelium, followed by their migration to fetal liver and to bone marrow. In zebrafish, kidney is the site of primary hematopoiesis. In humans, the presence of HSC in the fetal or adult kidney has not been established.MethodsWe analyzed the presence of HSC markers in human fetal kidneys by analysis of single-cell datasets. We then analyzed in kidney organoids derived from iPSC, the presence of hematopoietic markers using transcriptome analyses.Results12 clusters were identified of stromal, endothelial, and nephron cell type-specific markers in the two fetal stage (17 weeks) kidney datasets. Among these, expression of hematopoietic cells in Cluster 9 showed expression of primitive markers. Moreover, whole transcriptome analysis of our iPSC-derived kidney organoids revealed induction of the primitive hematopoietic transcription factor RUNX1 as found in the human fetal kidney cortex.ConclusionsThese finding support the presence of cells expressing HSC transcriptome in human kidney. The mechanisms of the appearance of the cells with the same transcriptional features during iPSC-derived kidney organoid generation requires further investigation.

Polarized Zeeman-effect flameless atomic absorption spectrometry of cadmium, copper, lead, and manganese in human kidney cortex.

1981 ◽  
Vol 27 (1) ◽  
pp. 68-72 ◽  
Author(s):  
P A Pleban ◽  
J Kerkay ◽  
K H Pearson
Keyword(s):  
Atomic Absorption ◽  
Zeeman Effect ◽  
Human Kidney ◽  
Absorption Spectrometry ◽  
Kidney Cortex ◽  
Flameless Atomic Absorption ◽  
Flameless Atomic Absorption Spectroscopy ◽  
Coefficients Of Variation ◽  
Cadmium And Lead ◽  
Copper Lead

Abstract We used polarized Zeeman-effect flameless atomic absorption spectroscopy to quantitatively measure cadmium, copper, lead, and manganese in a nitric acid digest of lyophilized human kidney cortex. Within-run coefficients of variation for cadmium, copper, lead, and manganese, 15.3, 177.2, 84.2, and 56.3 microgram/L, respectively, were 4.1, 6.3, 3.7, and 5.6%, respectively. Between-run coefficients of variation were 6.9, 5.5, 5.9, and 6.3%, respectively, for cadmium, copper, lead, and manganese concentrations of 135.1, 12.8, 2.72, and 3.80 microgram/g, respectively. For cadmium, copper, lead, and manganese digest concentrations (mean +/- SE) of 15.3 +/- 0.6, 41.4 +/- 2.6, 9.4 +/- 0.6, and 20.9 +/- 0.4 microgram/L, respectively, the detection limits were 5.2 microgram/L for copper, 1.2 microgram/L for both cadmium and lead, and 0.8 microgram/L for manganese. Assays were linear to 75 microgram/L for cadmium, 100 microgram/L for manganese, and 200 microgram/L for copper and lead. Average analytical recoveries for the four metals ranged between 95 and 101%. Because these metals were quantitated in the same digest of kidney cortex, the values for each digest gave a trace-metal profile for each autopsy specimen.

Zymographic approach to determine the intrinsic enzyme specific activity of diamine oxidase in presence of interfering enzymes

2017 ◽  
Vol 975 ◽  
pp. 78-85 ◽  
Author(s):  
Samaneh Ahmadifar ◽  
Tien Canh Le ◽  
Lucia Marcocci ◽  
Paola Pietrangeli ◽  
Mircea Alexandru Mateescu
Keyword(s):  
Diamine Oxidase ◽  
Specific Activity ◽  
Enzyme Specific Activity
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