Abstract
The chapter discusses the investigations according to which the specificity of sialyltransferases from different animal species and tissues varies appreciably. However, as a result of the lack of well-defined macromolecular sialic-acid acceptors, the study was difficult. The influence of several parameters of the acceptor substrate on enzyme activity has been studied: the nature of the accepting sugar, the distance of the acceptor sugar from the polypeptide chain, and the presence of hydrophobic arms between the sugar and the protein. In a study described in the chapter, lysozyme was chosen as protein. The various synthetic substrates were tested for N-acetylneuraminic acid acceptor activity. The sialyltransferase studies were carried out with particulate (microsome) enzyme preparations obtained from frog (Rana esculenta) and cow liver, and from pig and cow submandibular glands. As a result of examinations, it was deduced that in liver and porcine submandibular gland glycoproteins, sialic acids are found to be linked to galactose residues, whereas in bovine submandibular gland glycoproteins, sialic acids are mainly linked to N-acetylgalactosamine.
Sign-in/Register to access full text options 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a call
