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Biochemical Heterogeneity of Infantile Central Nervous System Spongy Degeneration

Department of Biological and Medical Research, King Faisal Specialist Hospital and Research Centre, Riyadh, Saudi Arabia

Aparna Tipirneni, BA

Department of Biological and Medical Research, King Faisal Specialist Hospital and Research Centre, Riyadh, Saudi Arabia

Nazih Youssef, BSc

Department of Biological and Medical Research, King Faisal Specialist Hospital and Research Centre, Riyadh, Saudi Arabia

Generoso G. Gascon, MD

Department of Pediatrics, King Faisal Specialist Hospital and Research Centre, Riyadh, Saudi Arabia

Pinar T. Ozand, MD, PhD

Department of Biological and Medical Research, King Faisal Specialist Hospital and Research Centre, Riyadh, Saudi Arabia, Department of Pediatrics King Faisal Specialist Hospital and Research Centre, Riyadh, Saudi Arabia

Aspartoacylase, the enzyme whose activity is deficient in infantile central nervous system spongy degeneration (Canavan-Van Bogaert-Bertrand disease), is detected as an approximately 59-kD protein in the Sephadex G-200 filtration of normal fibroblast extracts. The enzyme activity in homogenates of fibroblasts is protected by leupeptin, a protease inhibitor. In the absence of leupeptin, 90% of aspartoacylase activity is lost. In some patients with infantile spongy degeneration, no activity (less than 2%) can be detected. In some other patients with residual activity in fibroblasts, two separate peaks of enzyme are eluted with molecular weight corresponding to approximately 59 and 19 kD. Aspartoacylase activity in this latter group is protected to the same extent by the presence of leupeptin. However, the elution of two peaks is independent of the presence of leupeptin. This study indicates biochemical heterogeneity in the pathogenesis of infantile spongy degeneration. (J Child Neurol 1992;7(Suppl):S22-S25.)

Journal of Child Neurology, Vol. 7, No. 1 Suppl, S22-S25 (1992)
DOI: 10.1177/08830738920070010411


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