Hyaluronidase in human somatic tissues and urine: polymorphism and the activity in diseases.
Author(s) -
Berta FiszerSzafarz,
Patrick Vannier,
Anna Lityń́ska,
Liming Zou,
Barbara Czartoryska,
Anna TylkiSzymańska
Publication year - 1995
Publication title -
acta biochimica polonica
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.452
H-Index - 78
eISSN - 1734-154X
pISSN - 0001-527X
DOI - 10.18388/abp.1995_4663
Subject(s) - hyaluronidase , sialic acid , hyaluronic acid , synovial fluid , urine , endocrinology , medicine , gene isoform , chemistry , biology , enzyme , biochemistry , pathology , osteoarthritis , gene , genetics , alternative medicine
The polymorphism of hyaluronidase (EC 3.2.1.35) (Hyase) was studied on a hyaluronan-polyacrylamide gel. Liver, placenta, ovary and breast tissue were found to have 7 active isoforms while leukocytes and platelets 5 and fibroblasts displayed no hyaluronidase activity. In serum, synovial fluid and urine soluble the most acidic forms are present. Desialylation showed that most of the hyaluronidase isoforms differ in the content of sialic acid. In patients with rheumatoid arthritis, hyaluronidase activity in the synovial fluid varied from not detectable to very high. A partial deficiency was demonstrated in sera from some patients with dysostosis multiplex without mucopolysacchariduria. In I-cell disease, hyaluronidase activity in serum was as that in controls.
Accelerating Research
Robert Robinson Avenue,
Oxford Science Park, Oxford
OX4 4GP, United Kingdom
Address
John Eccles HouseRobert Robinson Avenue,
Oxford Science Park, Oxford
OX4 4GP, United Kingdom