1976
DOI: 10.1038/icb.1976.13
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Sulphatases, Lysosomes and Disease

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1978
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Cited by 54 publications
(18 citation statements)
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“…The intermediate band most likely represents a heteropolymer formed between human and hamster subunits in hybrid cells (24). This is consistent with the dimeric structure shown for ARSA by physical-chemical studies (25) …”
Section: Methodssupporting
confidence: 69%
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“…The intermediate band most likely represents a heteropolymer formed between human and hamster subunits in hybrid cells (24). This is consistent with the dimeric structure shown for ARSA by physical-chemical studies (25) …”
Section: Methodssupporting
confidence: 69%
“…Hybrids negative for human ARSB showed only the hamster band (channels 3 and 5). No heteropolymers of ARSB were observed, confirming the monomeric nature of this enzyme (25). Any hybrid showing the human band was scored positive for ARSB.…”
Section: Methodsmentioning
confidence: 64%
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“…Two of these, commonly known as arylsulphatases A and B (so called Type II enzymes) are hydrolases which are optimally active at an acid pH and are localized mainly in the lysosomal fraction of all the cells which contain them.They are also characterized by their relatively low activity towards esters of simple phenols (e.g. Roy, 1976) and enzyme B is probably involved in the controlled degradation of sulphated glycosaminoglycans of connective tissues (Gorham and Cantz, 1978). The third enzyme, known for many years as arylsulphatase C (a so called Type I enzyme), seems to be the only true mammalian arylsulphatase.…”
Section: Mammalian Arylsulphatasesmentioning
confidence: 99%