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Biomedical subjects

S Wood

Publications and source records attributed to S Wood.

At least 271 records · Page 15Linked to original sources
PubMed1977

Progressive cerebellar ataxia, spasticity, psychomotor retardation, and hexosaminidase deficiency in a 10-year-old child: juvenile Sandhoff disease.

During the course of investigating a 10-year-old boy because of progressive deterioration of intellectual functioning, ataxia, and hemiplegia, an absence of serum hexosaminidase activity was noted. A skin biopsy examined by electron microscopy showed axonal accumulations of dense osmiophilic deposits. Because of the patient's age at onset and the slowly progressive nature of his ilness, we are reporting an atypical juvenile case of Sandhoff disease.

Age Factors↗
PubMed1976

Cultured fucosidosis fibroblasts: a simple technique demonstrating storage of tritiated-fucose labeled material.

Incorporation of tritiated fucose into the acid-soluble and acid-insoluble fractions of cultured fucosidosis and control fibroblast monolayers was determined over a 10-day period. Fucosidosis cells incorporated significantly more label into the acid-soluble, but not the acid-insoluble fraction, than control cells. The ratio of acid-insoluble radioactivity increased lineraly from 1 to 10 days for the fucosidosis cells, indicating the storage of low molecular weight partial degradation products.

Carbohydrate Metabolism, Inborn Errors↗
PubMed1976

Juvenile Sandhoff disease: some properties of the residual hexosaminidase in cultured fibroblasts.

The residual hexosaminidase isoenzymes in juvenile Sandhoff and infantile Sandhoff disease fibroblasts, have been determined by starch gel electrophoresis and column isoelectric focusing. Hex A and hex S are the major residual isozymes in fibroblasts from the juvenile patient, while hex B is barely detectable. Only hex S could be detected in fibroblasts from infantile Sandhoff patients. These results suggest that the defects in juvenile and infantile Sandhoff disease may be different allelic modifications of the beta subunit common to hex A and hex B.

Electrophoresis, Starch Gel↗
PubMed1976

Plasma alpha-L-fucosidase: presence of a low activity variant in some normal individuals.

The expression of a variant alpha-L-fucosidase has been determined in both plasma and leukocytes. This variant enzyme is characterized by unusually tow actuvity in plasma, an altered pH activity profile, and increased heat lability. Individuals possessing this low activity variant in plasma have usual levels of alpha-L-fucosidase activity in leukocytes. The leukocyte enzyme also shows increased heat lability and has an altered pH activity profile. Gel filtration of plasma alpha-L-fucosidase revealed both a high molecular weight form, alpha-L-fucosidase I, and a low molecular weight form, alpha-L-fucosidase II. Only alpha-L-fucosidase II could be detected upon gel filtration of the variant enzyme from plasma. Both control and variant leukocyte alpha-L-fucosidase revealed two peaks by gel filtration but the proportion of alpha-L-fucosidase I was reduced in the variant enzyme sample. Alpha-L-fucosidase II from both control and variant plasma and leukocyte samples was heat labile and possessed little activity at pH 4.0 Alpha-L-fucosidase I from control plasma and leukocytes was more stable to heating and possessed more activity at pH 4.0 than alpha-L-fucosidase II. In contrast, alpha-L-fucosidase I from the variant leukocyte sample was heat labile and had little activity at pH 4.0 thus resembling alpha-L-fucosidase II. These results suggest that the variant is the consequence of an altered allele which affects alpha-L-fucosidase expression in all tissues.

Adult↗
PubMed1973

Gelatin: a poor substrate for a mammalian collegenase.

A rabbit tumor collagenase was purified more than 5000-fold. In this form it degrades native collagen in helical conformation at 37 degrees C, pH 7.6, into two fragments, but it had little capacity to cleave gelatin, an indication of the importance of higher-order structure of substrate for this enzyme in pure form. It is likely that, in vivo, enzymes other than collagenase degrade gelatin polypeptides produced by primary collagenolysis.

Animals↗