PRIMARY STRUCTURE OF THE MURINE MONOCLONAL IGG2A ANTIBODY MAB735 AGAINST ALPHA(2-8) POLYSIALIC ACID .2. AMINO-ACID-SEQUENCE OF THE HEAVY (H-)CHAIN FD' REGION
S. Klebert et al., PRIMARY STRUCTURE OF THE MURINE MONOCLONAL IGG2A ANTIBODY MAB735 AGAINST ALPHA(2-8) POLYSIALIC ACID .2. AMINO-ACID-SEQUENCE OF THE HEAVY (H-)CHAIN FD' REGION, Biological chemistry Hoppe-Seyler, 374(10), 1993, pp. 993-1000
The complete amino acid sequence of the Fd' region including the VH pa
rt, the CH1 domain, and the hinge segment of the biologically relevant
monoclonal mouse anti-alpha(2-8) polysialic acid antibody mAb735 is p
resented. The reduced and carboxymethylated H-chain was digested with
trypsin and cyanogen bromide. For subfragmentation selected peptides w
ere cleaved with thermolysin and endoproteinase Asp-N. The generated p
eptides were isolated by RP-HPLC and characterized by sequence analysi
s, plasma desorption mass spectrometry (PDMS), and amino acid analysis
. The N-terminal sequence was determined after enzymatic deprotection
with pyroglutamate aminopeptidase. According to Kabat et al. the varia
ble region of the H-chain belongs to the subgroup II. Sequence data fr
om the constant region indicate that mAb735 represents the gamma2a iso
type.