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Title
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Panulirus interruptus hemocyanin. The amino acid sequence of subunit b and anomalous behaviour of subunits a and b on polyacrylamide gel electrophoresis in the presence of SDS.
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Authors
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P.A.Jekel,
H.J.Bak,
N.M.Soeter,
J.M.Vereijken,
J.J.Beintema.
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Ref.
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Eur J Biochem, 1988,
178,
403-412.
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PubMed id
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Abstract
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The primary structure of subunit b of Panulirus interruptus hemocyanin has been
derived from two digests (trypsin and CNBr) and, in some cases, with aid from
the similarity with the sequence of subunit a. Differences between the amidation
states of Asx and Glx residues in subunit b relative to a were investigated more
thoroughly. When compared to the sequence of subunit a, 18 differences (2.7%)
were found and certain heterogeneities, indicating the presence of a minor
subunit b', were observed. Several differences in properties between subunits a
and b, including their anomalous behaviour on SDS/polyacrylamide gel
electrophoresis, could be explained by amino acid replacements.
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