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Biomedical subjects

S Shahangian

Publications and source records attributed to S Shahangian.

27 records · Page 2Linked to original sources
PubMed1984

Turbidimetric measurement of total urinary proteins: a revised method.

A turbidimetric method for the determination of total urinary proteins is proposed that uses a specimen blank for each urine. The precipitant, trichloroacetic acid (TCA), is introduced into the blank and the sample in the same amount. The blank is the supernatant of the TCA-treated urine for each specimen. Turbidity is measured by reading the 420-nm absorbance 35 minutes after the TCA addition when the turbidity curves for most urine samples plateau. This improved method was compared with an established procedure that uses water to prepare the blanks and that measures turbidity 5 minutes after the TCA addition. Of the 69 urine specimens that were analyzed by the two methods, the revised procedure yielded higher values (greater than or equal to 150%) for 5 samples, while 21 samples had lower values (less than or equal to 50%). In the latter group, four cases would have been classified erroneously as having significant proteinuria by the established method.

Humans↗
PubMed1984

Formate concentrations in a case of methanol ingestion.

An eight-month-old infant ingested at least 3.5 g of methanol when he accidentally received 5 mL of amoxicillin suspended in 70% methanol. The serum methanol concentration 8 h later was 9.7 mmol/L (310 mg/L) and the formate concentration 23 mmol/L (1.0 g/L). At 18 h after the ingestion, total CO2 had decreased to 6.8 mmol/L. Throughout the second day, 21-32 h after the ingestion, the methanol concentration was 2.8-3.4 mmol/L (90-110 mg/L) and that of formate was 31-33 mmol/L (1.4-1.5 g/L). On the third day, 46 h after the ingestion, methanol was not detected and the formate concentration had declined to 16 mmol/L (720 mg/L). The patient was treated with activated charcoal 7 h after the ingestion and with ethanol, administered both orally and intravenously, 21 h after the ingestion. No abnormalities of the infant's eyes were noted upon ophthalmological examination approximately 55 h after the incident.

Adult↗
PubMed1984

Creatine kinase and lactate dehydrogenase isoenzymes in serum of patients suffering burns, blunt trauma, or myocardial infarction.

Medical records of 53 burn and trauma patients were reviewed to assess the possibility of myocardial damage. Except for electrophoretically detectable creatine kinase MB isoenzyme, none showed evidence of myocardial injury. Lactate dehydrogenase isoenzyme tests, electrocardiograms, myocardial pyrophosphate scans, clinical course, and results of (two) autopsies were all negative for myocardial necrosis or ischemia. Types of patient, number, mean peak value (U/L) for serum creatine kinase, and ranges of percentage MB isoenzyme were as follows. Burns from direct electrical contact: 28, 16 600, 0-29; electrical flash or other thermal burns: 10, 4340, 0-22; blunt trauma (mostly from automobile accidents): 15, 3430, 0-18; myocardial infarction: 57, 1520, 4-46. Evidently creatine kinase MB isoenzyme is nonspecific in burn and trauma patients and should not be the only test result used to assess myocardial involvement.

Adolescent↗
PubMed1982

Isolation and characterization of horseradish peroxidase compound X.

Horseradish peroxidase reacts with sodium [36Clll] chlorite at pH 10.7 to form a 36Cl-labeled horseradish peroxidase intermediate. The optical absorption spectrum of this intermediate is quite stable and very similar to that of horseradish peroxidase Compound II. The intermediate can be separated from small molecules by chromatography on a Sephadex G-10 column. After fractionation, 65 to 93% of 36Cl in the reaction mixture remains associated with horseradish peroxidase. The remainder of 36Cl-labeled enzyme reacts with 5,5-dimethyl-2-chloro-1,3-cyclohexanedione (monochlorodimedone) at pH 4 to transfer 36Cl from the enzyme to the halogen acceptor molecule. [36C]5,5-Dimethyl-2,2-dichloro-1,3-cyclohexanedione (dichlorodimedone) was established as the major product of the transfer reaction by co-crystallization of the enzymic product with authentic dichlorodimedone and by thin layer chromatography. A chlorine oxide ligand on a ferryl heme iron protoporphyrin IX is proposed for the structure of Compound X.

Chemical Phenomena↗
PubMed1981

The reaction of chloroperoxidase with chlorite and chlorine dioxide.

Chloroperoxidase catalyzes the dismutation of chlorite-forming chloride, chlorine dioxide, chlorate, and oxygen as products. The yields of chlorine dioxide are variable because chloroperoxidase also catalyzes the decomposition of this compound and, in addition, moderate concentrations of chlorine dioxide inactivate the enzyme. Chloride, chlorate, and oxygen are the products of the decomposition of chlorine dioxide. The optimum pH for the enzymic of decomposition of both chlorite and chlorine dioxide is approximately pH 2.75. At this pH, 1 mole of chlorine dioxide is dismutated to 0.3 mole of chloride, 0.7 mol of chlorate, and 0.17 mole of oxygen. At the same pH, the complete decomposition of 1 mole of chlorite yields 0.4 mole of chloride, 0.6 mole of chlorate, and 0.13 mole of oxygen. During the inactivation of chloroperoxidase by chlorine dioxide, the Soret absorption band of the native enzyme is completely lost, and the enzyme becomes chlorinated. Kinetic parameters for the chlorite reaction have been determined. The Km value for chlorite obtained from various kinetic plots was about 10 mM. The catalytic rate constant for the formation of chlorine dioxide from chlorite was about 70,000 s-1.

Chloride Peroxidase↗
PubMedDate not supplied

An enzymatic method for the analysis of formate in human plasma.

An enzymatic method for the determination of plasma formate concentration is described. Formate dehydrogenase is used to reduce NAD+ to NADH in the presence of formate. The resulting NADH then reduces the dye resazurin to resorufin, a reaction catalyzed by the endogenous diaphorase of the plasma. The generated resorufin is then measured fluorimetrically by exciting it at 565 nm and quantitating the emitted light at 590 nm. The method uses the patient's plasma as the blank and as the matrix for the construction of a patient-specific formate calibration curve. The blank contains all components of the assay system except the formate dehydrogenase. Formate concentration is determined from the calibration curve, constructed by adding known quantities of sodium formate to the plasma base, and plotting the fluorescence intensity against formate concentration. The assay which is sensitive to a formate level of 7 mg/L should find application in cases where formate is a metabolite.

Aldehyde Oxidoreductases↗