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Biomedical subjects

G Porcelli

Publications and source records attributed to G Porcelli.

At least 37 records · Page 2Linked to original sources
PubMed1986

Kallikrein and kininase activities excretion in newborns affected by jaundice.

In a homogeneous group of 30 newborns, aging between 10 hours--10 days, and affected by jaundice, urinary kallikrein and kininase activities were determined. The variable considered were: sex, time of life, weight and gestational age. Urinary samples were taken at the beginning and at the end of phototherapy.

Birth Weight↗
PubMed1986

Kallikrein and kininase excretion in football players after psychophysical stress.

In eleven football players and in four football-reserve players urinary kallikrein and kininase activities were determined before and after an official match. The results showed a significant reduction of kallikrein after the match in football players when the football-reserve players were used for comparison (p less than 0.01). Kininase activity appears increased in football players after the match, but not significantly. The Kininase/Kallikrein ratio after the match resulted significantly increased in football players (p less than 0.05) and very significantly compared to the football-reserve players (p less than 0.01).

Adult↗
PubMed1984

A young girl with ring(18) mosaicism: cytogenetic studies and PEP A mapping.

A young girl with 46,XX,r(18)/46,XX/45,XX,-18 chromosome constitution is reported. She displays a slight degree of mental retardation. The line with the ring chromosome predominates in blood lymphocytes. In skin fibroblast culture the ring(18) line showed a constant decreasing trend, from 45% at the first passage, down to its disappearance at the 19th passage, where only 46,XX cells were observed. The child/mid parents' ratio of Peptidase A activity in red cells was 0.36. The Peptidase A activity in a fibroblast clone 46,XX,r(18) was 0.55 compared to the 46,XX line. These data suggest that the PEP A locus was lost in ring formation.

Adolescent↗
PubMed1981

Urinary kallikrein and hypertension in cadmium-exposed rats.

Chronic exposure of rats to cadmium (Cd) in drinking water induced elevated systolic and diastolic blood pressure. Heart rate, however, was lowered, suggesting that the hypertension in these rates may be due to an increase of the total peripheral resistance, possibly involving a central nervous system (CNS) component in Cd-induced hypertension. Urinary kallikrein activity was reduced in the exposed animals and may explain the previously reported antinatriuretic effect of Cd, since renal kallikrein is an enzyme responsible for the synthesis of kallidin, a potent vasodilator and natriuretic polypeptide.

Animals↗
PubMed1979

Method for measurement of human urinary kininase activity.

A method was developed to measure kininase activity in human urine. The method consists of dialysis of human centrifuged urine sample against phosphate buffer and partial fractionation of A-50 Sephadex column. The enzymatic property of urinary kininase, which destroys bradykinin when incubated, is estimated from its effect on a definite amount of bradykinin, using rat uterus.

Animals↗
PubMed1979

Chemical relations between renal and urinary kallikrein of rat.

The ratio in micron-Moles between each aminoacid residue of both hydrolized renal and urinary kallikrein of rat, is about 1.00 +/- 0.3. Except for Glu, His and Glucosamine a good proportion between all residues of both enzymes was obtained. It is probable that the different molecular weight, respectively 40,000 for the renal kallikrein and 32,000 for the urinary enzyme, is an artefact of the different procedures used for the purification of rat kallikrein.

Amino Acids↗
PubMed1979

Purification of horse renal kallikrein and chemical relations with horse urinary kallikrein.

Kallikrein was purified from horse kidney by several steps of chromatographic procedure and by affinity chromatography on Sepharose-Concanavaline. Horse urinary kallikrein was previously purified by DE-32 hydroxylapatite and by Sephadex G-100 gel filtration. On the purified final sample of renal and urinary kallikrein the aminoacid composition and the gel electrophoretic molecular weight were determined. The ratio in micronMoles between each aminoacid residue of both hydrolyzed renal and urinary kallikrein of horse is about 1,00 +/- 0,30. Except for Pro, 1/2 Cys and basic aminoacid residues a good proportion was obtained. It is confirmed that the different molecular weight, respectively 47,500 for renal kallikrein and 28,000 for the urinary enzyme is an artefact of the different procedures used for the purification of horse kallikrein.

Amino Acids↗
PubMed1979

Altered urinary excretion of human kininase activity in acute myocardial infarction.

This study concerns the determination of levels of human urinary kininase excretion in acute myocardial infarction (AMI). The results obtained by a biological method show that there is a significant reduction of the enzymatic activity in patients affected by AMI in comparison with normals (6.4 +/- 0.4 ng of destroyed bradykinin/min. versus 164.4 +/- 31.4 ng; P less than 0.001), while urinary kallikrein excretion was close to normal values.

Humans↗
PubMed1979

Tests to localize free proteolytic enzymes in vivo by 14C-cysteine-aprotinin.

Aprotinin, a polyvalent protease inhibitor from bovine organs, has been labelled with 14C-cysteine in 6 M urea to produce a radioactive conjugate, without effect on the inhibitor activity. 138x10(3) dpm of radioactive product, containing 5 mg of protein (20.000 kal. inhibitor units) in 5 ml of Locke's solution were perfused in anesthetized rabbits via ascending aorta. Then the anesthetized rabbit was killed and specimens of some organs were admitted to autoradiographic analysis. Small intestine, ischiatic nerve and testis have been the most rich radiolabelled organs (+++). In kidney, stomach, large intestine, liver and eye the radiolabelled aprotinin was found in fair amounts (++); while in pancreas, spleen, spinal cord, brain, cava vein and aorta of rabbit the 14C-cysteine-Aprotinin was practically undetectable by autoradiography.

Animals↗