�ber die physiologische Polysaccharidausnutzung bei jungen S�uglingen

Kleinbaum, H

doi:10.1007/bf00439692

Cited by 5 publications

(1 citation statement)

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“…White measured glucose in honey by a photometric procedure in which contaminant invertase was inhibited by tris buffer (350), and Tengstrom (328) determined both glucose and galactose in urine. Kleinbaum (155) proposed a single method for the determination of galactose in biological fluids, and Hjelm (126) used a galactose oxidase-peroxidase-o-dianisidine reagent for the determination of galactose in whole blood, plasma, and erythrocytes.…”

Section: Determination Of Substratesmentioning

confidence: 99%

Use of enzymes in analytical chemistry

Guilbault¹

1968

Anal. Chem.

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Both of these contain valuable procedures for enzyme analysis. Guilbault (97) has authored a chapter on fluorometric methods of analysis of enzymes, substrates, activators, and inhibitors in his book, "Fluorescence. Theory, Instrumentation and Practice." Passwater's book,(233) "Guide to the Umbelliferone (7 -hydroxy coumarin) and 4-methyl-umbelliferone are highly fluorescent compounds which have been modified to form nonfluorescent substrates for the enzymes glucuronidase, glucosidase, Ar-acetyl-/3-glucosaminidase, and ß-galactosidase. Robinson (259) used 4-methylumbelliferone^-Dglucoside as a substrate for ß-glucosidase. The substrate is split specifically by this enzyme, thus permitting the separate identification of ß-glucosidase and ß-glucuronidase in paper electrophoresis. Woolen and Turner (358, 359) assayed ß-glucuronidase in plasma using 4-methyl umbelliferylß-glucuronide as substrate, and Woolen and Walker (360), proposed 4-methyl umbelliferone-.Y-acetyl -ß-D-glucosaminide and 4-methyl umbelliferone-ß-D-galactoside as substrates for V-acetylß-D-glucosaminidase and ß-galactosidase. Likewise, Leaback (169) described conditions for the continuous fluorometric assay of Y-acetyl^-Dglucosaminidase using the same substrate, and Veritz, Gambell, and Brown (336) proposed l-naphthyl-2-acetamido-2-deox3T^-D-glucop3"ranoside as a substrate for this enzyme. The production of 1-naphthol was proportional to the concentration of enzyme.Greenberg (96) assayed ß-glucuroni-

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Section: Determination Of Substratesmentioning

confidence: 99%

Use of enzymes in analytical chemistry

Guilbault¹

1968

Anal. Chem.

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The influence of conditioned reflexes on the activity of ?-amylase in the saliva of healthy children

Kleinbaum

Etzold

1970

Z. Kinder-Heilk.

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Die ?-Amylase-Aktivit�t im Harn gesunder Schulkinder

Kleinbaum

Schmidt

1970

Z. Kinder-Heilk.

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The a-amylase Activity in the Urine o/Healthy School Children Summary. The introduction of new laboratory methods requires a review of the "normal values". The micro-and ultra micro method for the determination of a-amylase activity by Street and Close, already used successfully by many laboratories, allows the determination of enzyme activity in many biological fluids but calls for a re-assessment of the so-called "normal values". In this study the results of determinations done on 210 school children are presented. The tests were perfomed with urine samples from a three hour period, collected under standard conditions. An exact statement of the quantity of a-amylase excreted with the urine per unit of time was thus made possible.The 210 children belonged to two age-groups: either 7--8 or 11--12 years old. The three parameters determined from the three hour sample were: Quantity, specific weight, and a-amylase activity. We were able to confirm our own earlier findings that the enzyme activity increases with age, in both, activity and quantity. Significant sex-dependent differences were not observed. The normal range of values of a-amylase concentration in urine was found to be between 40 and 250 SCU (Street-Close Units) per 100 ml urine and the total excretion within three hours ranged from 25--200 SCU. A correlation between a-amylase concentration and specific weight of the urine was not observed. This form of test implies an improvement of the diagnostic possibilities.~chliisselw6rter: a-Amylase im Urin --Normalwerte --gesunde Schulkinder.Die Einffihrung neuer Methoden in die klilfischen Laboratorien macht die st~ndige Uberarbeitung und Ergi~nzung der j eweiligen ,,Normalwerte" erforderlieh. Die bereits in vielen Kliniken angewandte Mikro-und Ultramikromethode yon Street u. Close [15,17] zurBestimmung der a-AmylaseAktivi~t in verschiedenen biologisehen Fliissigkeiten macht die Aufstellung eines kompletten Ka~aloges yon Normalwerten dieser Hydrolase in den einzelnen K6rperfliissigkeiten notwendig.Die a-Amylase, 3,2,1,1-a-1,4-Gluean-4-glueanohydrolase, ist ein Me. talloenzym, als dessen Stabilisator Calcium fungiert. Das Molekfil bes~eh~ aus 18 Aminos~uren, vorwiegend Glyein, Lysin, Arginin und Aspar~gin. Ffir die Ak~ivit~t des Enzyms sind seine prim~ren Aminogruppen yon besonderer Bedeutung, die Hydroxylgruppen k61men da-

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�ber die physiologische Polysaccharidausnutzung bei jungen S�uglingen

Cited by 5 publications

References 15 publications

Use of enzymes in analytical chemistry

Use of enzymes in analytical chemistry

The influence of conditioned reflexes on the activity of ?-amylase in the saliva of healthy children

Die ?-Amylase-Aktivit�t im Harn gesunder Schulkinder

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