To improve security and privacy, we are moving our web pages and services from HTTP to HTTPS. To give users of web services time to transition to HTTPS, we will support separate HTTP and HTTPS services until the end of 2017. From January 2018 most HTTP traffic will be automatically redirected to HTTPS. [more...] View this page in https
α-lactalbumin , a milk protein, is the regulatory subunit of lactose
synthase. In the mammary gland, α-lactalbumin changes the substrate
specificity of galactosyltransferase from N-acetylglucosamine to glucose.
Lysozymes (EC 22.214.171.124)  act as bacteriolytic enzymes by hydrolyzing the
β(1->4) bonds between N-acetylglucosamine and N-acetylmuramic acid in the
peptidoglycan of prokaryotic cell walls. There are at least five different
classes of lysozymes [3,4]: C (chicken type), G (goose type), phage-type (T4),
fungi (Chalaropsis), and bacterial (Bacillus subtilis) but there are few
similarities in the sequences of the different types of lysozymes.
α-lactalbumin and lysozyme C are evolutionary related . Around 35 to
40% of the residues are conserved in both proteins as well as the positions of
the four disulfide bonds (see the schematic representation). The pattern for
this family of proteins includes three cysteines involved in two of these
disulfide bonds (the first cysteine is linked to the third one).
PROSITE is copyright. It is produced by the SIB Swiss Institute
Bioinformatics. There are no restrictions on its use by non-profit
institutions as long as its content is in no way modified. Usage by and
for commercial entities requires a license agreement. For information
about the licensing scheme send an email to
or see: prosite_license.html.