Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:3.2.1.36 (hyaluronidase)
 4,606 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Hyaluronan was substituted with tyramine-cellobiose on amino residues exposed after hydrazinolytic N-deacetylation of the polysaccharide. Nonsubstituted amino groups were reacetylated, and the carboxylic hydrazides were removed by treatment with HIO3. The adduct was labeled with 125I before or after coupling to hyaluronan. N-deacetylation increased with prolonged pretreatment with hydrazine, which also reduced the chain length of hyaluronan. Hydrazinolysis for 30 min produced hyaluronan with Mr 2.2-2.9 x 10(5). This material was substituted with varying amounts of tyramine-cellobiose (from 1 per 20 to 1 per 130 disaccharides). Hyaluronan labeled in this way was recognized by Streptomyces hyaluronidase, hyaluronan affinity protein of cartilage proteoglycan, and receptors for specific endocytosis of hyaluronan in liver endothelial cells. Since tyramine-cellobiose is nondegradable and therefore is arrested intralysosomally at the site of uptake, turnover studies of hyaluronan can be easily carried out with this ligand.
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PMID:Preparation of biologically intact radioiodinated hyaluronan of high specific radioactivity: coupling of 125I-tyramine-cellobiose to amino groups after partial N-deacetylation. 307 Nov 84