Protein bromination by bromoperoxidase from Penicillus capitatus
JA Manthey, LP Hager, KD McElvany - Methods in enzymology, 1984 - Elsevier
Publisher Summary Myeloperoxidase (MPO) and bromoperoxidase (BPO), isolated from
crude algal extracts of P. capitatus, provide excellent systems for enzymatic radiolabeling of
proteins. MPO and BPO are active at neutral pH. Both MPO and the BPO preparations
catalyze bromination mainly at tyrosine residues in canine fibrinogen and human serum
albumin (HSA). The brominated canine fibrinogen retains all the clotting activity associated
with the native protein and no detectable change in biological activity occurs upon the …
crude algal extracts of P. capitatus, provide excellent systems for enzymatic radiolabeling of
proteins. MPO and BPO are active at neutral pH. Both MPO and the BPO preparations
catalyze bromination mainly at tyrosine residues in canine fibrinogen and human serum
albumin (HSA). The brominated canine fibrinogen retains all the clotting activity associated
with the native protein and no detectable change in biological activity occurs upon the …