Journal
BIOCHEMISTRY-MOSCOW
Volume 71, Issue 3, Pages 251-261Publisher
MAIK NAUKA/INTERPERIODICA/SPRINGER
DOI: 10.1134/S0006297906030047
Keywords
antibodies; natural abzymes; AIDS; proteolytic activity
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Proteolytic activity of polyclonal IgG antibodies (Abs) from the blood of AIDS patients was analyzed for the first time. These Abs were shown to display higher activity in hydrolysis of P-casein than in hydrolysis of human immunodeficiency virus (HIV)-1 reverse transcriptase (RT) or human serum albumin (HSA). Several abzymatic criteria were applied and it was shown that RT, HSA, and beta-casein hydrolyzing activities are an intrinsic property of polyclonal Abs from AIDS patients. Casein-hydrolyzing Abs were detected in the blood serum for 9596 of AIDS patients, and it was shown that they possess serine protease-like catalytic activity. The substrate specificities of polyclonal Ab proteases and typical human proteases are different. Depending on the patient, the IgGs exhibit various pH optima of proteolytic activity. The products of casein hydrolysis by Ab proteases were different from those in the case of trypsin, chymotrypsin, and proteinase K.
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