Arginase and Free Amino Acids in Hyperargininemia: Leukocyte Arginine as a Diagnostic Parameter for Heterozygotes

Marescau, B.; Pintens, J.; Löwenthal, A.; Terheggen, H. G.; Adriaenssens, K.

doi:10.1515/cclm.1979.17.4.211

Cited by 2 publications

(2 citation statements)

References 15 publications

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“…erythrocytes (2)(3)(4) and leukocytes (5). In this paper Argininaemia is an inborn metabolic disorder of the we report deficient arginase activity in the saliva of urea cycle dtie to arginase (L-arginine-homozygous patients, together with our fmdings on amidinohydrolase, EC 3.5.3.1) deficiency.…”

Section: Introductionmentioning

confidence: 56%

Human Salivary Arginase and Its Deficiency in Argininaemia

Konarska¹,

Tomaszewski²,

Colombo³

et al. 1985

Clinical Chemistry and Laboratory Medicine

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Arginase from normal human mixed saliva was characterized. The enzyme was completely activated after a preincubation of 20min at 55 °C and a Mn 2+ final concentration of 5 mmol/1. The pH Optimum was 9.6-9.8, and the K m for L-arginine was 4.2 ± 0.7 mmol/1. In normal saliva only one form was found, which was chromatographically identical with the cationic form of arginase in liver and blood cells. Salivary arginase was completely precipitated by rabbit aiitiserüm against human liver arginase.Arginäse activity was not detectable in the saliva of patients suffering from argininaemia. Enzyme activities in the saliva of the heterozygous parents and the unaffected daughter were 0.08, 0.07 and 0.12 U/mg protein, respectively, whereas the activities in the saliva of 60 healthy adults and 8 children were 0.17 + 0.11 and 0.16 ± 0.06 U/mg protein, respectively. Menschliche Speichel·Arginase und ihr Fehlen bei der ArgininämieZusammenfassung: Die aus gemischtem Speichel gewonnene Arginase wurde charakterisiert. Nach Präinkubation von 20 min bei 55 °C und einer Mn*~ Endkonzentration von 5 mmol/1 wird das Enzym voll aktiviert. Das pH-Optimum lag zwischen 9,6-9,8; der Äm-Wert für Arginin betrug 4,2 + 0,7 mmol/1. Im normalen Speichel konnte nur eine Form der Arginase gefunden werden. Diese ist chromatographisch identisch mit der kationischen Form der Lebere und Erythrocytenarginäse. Die Speichelarginase wird durch gegen menschliche Leberarginase gerichtetes Kaninchenserum vollständig prä_zipitiert.Im Speichel von Patienten mit Argininämie konnte keine Arginaseaktivität nachgewiesen werden. Die Enzymaktivität im Speichel der heterozygoten Eltern betrug 0,08 resp. 0,07, diejenige der gesunden Schwester 0,12 U/mg Protein. Im Speichel von 60 gesunden Erwachsenen fand sich eine Aktivität von 0,17 ± 0,11, bei 8 Kindern eine solche von 0,16 ± 0,06* U/mg Protein.

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Section: Introductionmentioning

confidence: 56%

Human Salivary Arginase and Its Deficiency in Argininaemia

Konarska¹,

Tomaszewski²,

Colombo³

et al. 1985

Clinical Chemistry and Laboratory Medicine

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“…The deficient arginase activity has been demon strated in the liver, red blood cells [2] and in white blood cells [3] of patients suffering from hyperargininemia.…”

Section: Introductionmentioning

confidence: 99%

Isoenzyme Pattern and Immunological Properties of Arginase in Normal and Hyperargininemia Fibroblasts

Konarska¹,

Wiesmann²,

Fellenberg³

et al. 1983

Enzyme

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Arginase deficiency is an inborn error of the last step in the urea cycle and leads to profound hyperargininemia. The enzyme deficiency has been demonstrated in the liver and red blood cells. In cultured patient fibroblasts, the activity is normal. Arginase exists in multiple molecular forms only one of which is missing in hyperargininemic patients. In fibroblasts, three arginase isoenzymes can be demonstrated by DEAE-cellulose column chromatography, two by electrophoresis and by immunoprécipitation methods. From the present data, it is improbable that part of the Ai isoenzyme in fibroblasts originates from fetal calf serum arginase which supplements the culture media. None of the techniques for the separation and analyses of arginase isoenzyme allows to differentiate between the normal and the arginase-deficient phenotype. A possible explanation would be that the defect in Aj arginase observed in the liver is the result of a regulatory defect.

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Arginase and Free Amino Acids in Hyperargininemia: Leukocyte Arginine as a Diagnostic Parameter for Heterozygotes

Cited by 2 publications

References 15 publications

Human Salivary Arginase and Its Deficiency in Argininaemia

Human Salivary Arginase and Its Deficiency in Argininaemia

Isoenzyme Pattern and Immunological Properties of Arginase in Normal and Hyperargininemia Fibroblasts

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