Testes, sialidase

Lysosomal sialidases are always copurified with P-galactosidase when isolated from tissues such as bovine testis (Verheijen et aL, 1982), porcine testis (Yamamoto and Nishimura, 1987), and human placenta (Verheijen et aL, 1985, 1987 Hiraiwa et aL, 1987, 1988). This sialidase-P-galactosidase complex can... 

Most lysosomal sialidases preferentially catalyze the hydrolysis of the a2-3-linked sialic acids compared to the a2-6 residues. Exceptions to this are the enzymes from rabbit spermatozoal acrosomes (Srivastava and Abou-Issa, 1977) and human liver (Michalski et aL, 1982), which are more active on a2-6-linked sialic acids on glycoproteins, i.e., Cowper s gland mucin or submandibular gland mucin. The enzymes from human liver and porcine testis are more active on a2-8-linked sialic acids in colominic acid than other lysosomal enzymes (Table III). 

Yamamoto, Y., and Nishimura, K., 1987, Copurification and separation of p-galactosidase and sialidase from porcine testis, Int. J. Biochem. 19 435-442. 

Other organs which have been reported to have sialidase activity are rat liver (Mahadevan et aL, 1967), rat and rabbit kidneys (Mahade-van et al., 1967 Kirschbaum and Bosmann, 1973 Kuratowska and Kubicka, 1967), ram testis (Roston et al., 1%6), human intestinal... 

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