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Biomedical subjects

M Aminlari

Publications and source records attributed to M Aminlari.

13 recordsLinked to original sources
PubMed2000

Distribution of rhodanese in different parts of the urogenital systems of sheep at pre- and post-natal stages.

The enzyme rhodanese (thiosulfate:cyanide sulfurtransferase) is a ubiquitous enzyme present in all living organisms, from bacteria to humans and plays a central role in cyanide detoxification. The purpose of this investigation is to determine and compare rhodanese activity in different parts of urogenital systems of male and female sheep fetuses at 2.5, 3, 3.5, 4, 4.5, and 5 months of age. The highest activity of rhodanese in male fetus was in kidney cortex, followed by medulla of the kidney. No significant difference was observed in other organs. In female fetus, the highest activity was in kidney cortex followed by oviduct and medulla of kidney. The enzyme activity of tissues increased with age. There was no significant difference (P > 0.05) between male and female fetuses in levels of rhodanese activity of different tissues except in urinary bladder at 2.5 and 3 months and in urethra at 4.5 months of age. The results of this study might indicate the involvement of rhodanese in cyanide detoxification in tissues which are more exposed to cyanide. On the other hand, rhodanese might perform other functions which are specific in these tissues.

Animals↗
PubMed1997

Rhodanese (thiosulfate: cyanide sulfurtransferase) in the digestive tract of chicken at different stages of development.

This study was undertaken to investigate the relationships between stage of embryonic development and early posthatch growth and the level of rhodanese (thiosulfate:cyanide sulfurtransferase) activity in different regions of the digestive tract and liver of chickens. The embryos were studied at 14, 17, and 20 d and chickens were 1, 2, and 3 wk old. All tissues studied contained rhodanese. The highest specific activity of rhodanese was present in the liver followed by the proventriculus (P < 0.05). The lowest level was in the esophagus. The level of rhodanese was found to increase with age in the proventriculus and duodenum. The highest rhodanese activity in 3-wk-old chickens was in the proventriculus followed by the liver. These results are discussed in terms of the role of different sections of the digestive tract of the chicken in cyanide metabolism.

Aging↗
PubMed1996

Isoprenaline induces biosynthesis of proline-rich proteins in the salivary glands of rat but not in sheep.

Long-term treatment of rats with isoprenaline resulted in induction of proline-rich proteins (PRPs) in the salivary glands, which were subsequently purified by TCA solubility and column chromatography. When rats were removed from beta-agonist regimen, then these proteins were no longer observed. Treatment of sheep with isoprenaline did not reveal the induction of PRPs.

Adrenergic beta-Agonists↗
PubMed1994

The cyanide-metabolizing enzyme rhodanese in different parts of the respiratory systems of sheep and dog.

Studies on the rhodanese activity of respiratory systems of sheep and dog showed that a significant difference exists in the pattern of distribution of this enzyme in different parts of the respiratory system of both species. In sheep, larynx, trachea, bronchiole, and lung contain higher activity than nasal cavity and pharynx. In dog, significantly greater rhodanese activity was found in nasal cavity than in other parts of the respiratory system. In regions with high rhodanese activity the enzyme was more concentrated in the mucosa than in the underneath tissues. These results are discussed in terms of the possible role of rhodanese in cyanide metabolism in respiratory tract and the efficacy of this organ in inhaled cyanide detoxification in these species of animals.

Animals↗
PubMed1994

Changes in arginase, aminotransferases and rhodanese in sera of domestic animals with experimentally induced liver necrosis.

Changes in the serum concentrations of aspartic aminotransferase (AST), alanine aminotransferase (ALT), rhodanese and arginase were measured in dogs, sheep and cattle with hepatic necrosis induced by the oral administration of carbon tetrachloride. A new method for arginase assay was based on the determination of remaining arginine (after its conversion to urea and ornithine) by its reaction with p-nitrophenyl glyoxal (PNPG). In all species studied the serum arginase increased 6-12 h after liver damage, reached a peak value in 48 h and returned to normal thereafter. Rhodanese activity did not change in dogs but rose significantly in sheep and, to a lesser extent, in cattle. AST increased strikingly in sheep as compared with dogs and cattle and remained high for > 5 days. In dogs ALT rose sharply and remained elevated for > 10 days. No change in ALT was seen in sheep or cattle. The determination of arginase by a simple procedure such as the PNPG method, in conjunction with AST or ALT assay, may be of value in assessing the stage of liver necrosis.

Animals↗
PubMed1994

Rhodanese (thiosulfate:cyanide sulfurtransferase) distribution in the digestive tract of chicken.

In this study the level of rhodanese (thiosulfate:cyanide sulfurtransferase) activity in different regions of the digestive tract of chicken was determined and compared with that in the liver, heart, kidney, and lung. All tissues studied contained rhodanese. The highest specific activity of rhodanese was in the submucosal layer of proventriculus, followed by liver, heart, the mucosal layer of cecum, rectum, and kidney. The lowest level was present in lung. These results suggest that in the chicken part of the ingested cyanide is detoxified in the digestive tract, mainly by the proventriculus, and part of the absorbed cyanide is metabolized by hepatic rhodanese.

Animals↗
PubMed1992

A novel colorimetric method for assaying arginase activity.

Arginase catalyzes the conversion of arginine to urea and ornithine in the liver of ureotelic animals. Higher activity of this enzyme is found in tumors as well as in the sera of patients with hepatic diseases. We have developed a simple colorimetric method for its determination. This is based on the determination of residual arginine, after its conversion with p-nitrophenyl glyoxal (PNPG) at pH 9.0 in the presence of sodium ascorbate. The reaction product obeys Beer's law in the range of 0.01-0.20 mmol/L arginine with an arginine-equivalent molar extinction coefficient of 0.65 x 10(4) M-1 cm-1. The decrease in absorbance in the presence of arginase correlates with the enzyme activity. Color development as well as termination of enzyme activity is achieved by addition of a single reagent, thereby obviating the use of many chemicals necessary in other methods. The sensitivity of this method is equivalent to those of currently available procedures but has the added advantages of greater convenience.

Arginase↗
PubMed1992

Arginase distribution in tissues of domestic animals.

1. A new colorimetric method was used for determination of arginase in different tissues of some domestic animals. 2. In all species studied liver was the richest source of arginase. 3. Significant differences were observed in the specific activity of arginase in livers from different species. 4. In all species, besides liver, kidney and brain also contained significant levels of arginase. 5. In the dog, in addition to the three organs mentioned above, lung, heart, spleen and skeletal muscle showed some arginase activity. 6. In sheep and cattle significant arginase activity was observed in the rumen. No differences were observed between epithelial and muscular layers of different parts of digestive system in all species studied. 7. These results are discussed in terms of the possible role of arginase in different tissues of animals.

Animals↗
PubMed1991

Comparative studies on the distribution of rhodanese in different tissues of domestic animals.

1. The activity of rhodanese in different tissues of some domestic animals was measured. 2. Rhodanese was present in all tissues studied. 3. The activity of rhodanese in most tissues of sheep was higher than other animals studied. 4. In sheep and cattle the epithelium of rumen, omasum and reticulum were the richest sources of rhodanese. Significant activity of rhodanese was also present in liver and kidney. 5. In camel the liver contained the highest level of rhodanese followed by lung and rumen epithelium. Camel liver contained a third of the activity of sheep liver. 6. Equine liver had a third of the activity of sheep liver. Other tissues showed low levels of rhodanese activity. 7. Dog liver contained only 4% of the activity of sheep liver. In this animal, brain was the richest source of rhodanese. 8. The results are discussed in terms of efficacy of different tissues of animals in cyanide detoxification.

Animals↗
PubMed1990

Determination of creatine kinase in the sera of patients with myocardial infarction by a rho-nitrophenylglyoxal method.

We have developed a new colorimetric method for the determination of creatine kinase (CK). This method is based on the reaction of creatine, formed enzymatically from creatine phosphate and ADP, with rho-nitrophenylglyoxal (PNPG) under mild alkaline conditions to produce a coloured complex which absorbs maximally at 480 nm. This method was applied to the sera of patients with myocardial infarction. The results obtained by the PNPG method agreed well with the results obtained by other available methods for CK. However, the PNPG method was more convenient and less expensive than other methods and required a single chromogenic reagent. The PNPG method might be easily adapted to routine clinical application.

Adenosine Diphosphate↗
PubMed1989

Comparative studies on the distribution of rhodanese and beta-mercaptopyruvate sulfurtransferase in different organs of sheep (Ovis aries) and cattle (Bos taurus).

1. The activities of rhodanese and beta-mercaptopyruvate sulfurtransferase (MST) in different organs of sheep and cattle were measured. 2. Liver, kidney, omasum, and rumen were the richest sources of both enzymes. The activities of both enzymes in other organs of the sheep and the cattle decreased in the order of lung, brain, heart, abomasum, lymph node, urinary bladder, spleen, and the skeletal muscle. 3. The activities of both enzymes in most organs of the sheep were higher than the cattle. 4. Both enzymes showed higher activities in the epithelial layers than the muscular layers of rumen, omasum and reticulum. 5. In most of the tissues of both species the level of rhodanese activity was greater than MST.

Animals↗
PubMed1987

A new colorimetric method for determination of creatine phosphokinase.

A new colorimetric method has been developed for the determination of creatine phosphokinase (CPK). This method is based on the reaction of creatine, formed enzymatically from creatine phosphate and ADP, with p-nitrophenylglyoxal (PNPG) under alkaline conditions to produce a colored product which absorbs maximally at 480 nm. At 25 degrees C the reaction was complete after 10 min in 0.1 M sodium pyrophosphate, pH 12, containing 0.15 M sodium ascorbate. The colored product was stable for at least 24 h and obeyed Beer's law in the range 0.005-0.05 mM creatine. The color reaction was used to determine the activity of CPK in serum and tissue extracts. The results obtained by this method agreed well with the results obtained by other available methods for CPK determination. However, the PNPG method was more rapid and more sensitive than other colorimetric methods and required a single chromogenic reagent.

Animals↗