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KMID : 0903519700130010059
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Journal of the Korean Society of Agricultural Chemistry and Biotechnology
1970 Volume.13 No. 1 p.59 ~ p.64
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Purification and N - Terminal Study of Bence Jones Proteins
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Abstract
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Human Bence Jones Protein could be purified by DEAF-Sephadex A-50 column (2×37㎝) with 0.02M phosphate Buffer (pH 8.0) and gradient increasing with NaCl concentration as in Fig. 2-4.
Sample As (K-type Bence Jones Protein) had two component, F-I was major component and its dried weight was 350㎎. of starting material of 500㎎.
Other Sample Im and Ik (λ-type Bence Jones Protein) was purified by DEAE-Sephadex A-50 with 0.02M phosphate Buffer(pH 8.0)too. F-I (major component) of Im and F-I of Ik were 242㎎ and 146㎎. its dried weight respectively. K-type of Bence Jones Protein´s(As, Ko, Ta.) N-terminal amino acid residue was determined by method of DNP,. K-type of Bence Jones Protein´s amino acid residue were either glutamic acid or aspartic acid.
Sample Ta was confirmed as glutamic acid its N-Terminal. As and Ko were aspartic acid.
Each yellowish spot (DNP-amino acids) were extracted with 4㎖. of pH 8.05% NaHCO₃ solution and calculated its recovery by O.D. (360mμ)using the ε=18.1×10³-DNP Asp.
ε=17.4×10³ DNP Gla. considering 50% lose during; the acid (6N-HCI) hydrolysis. Recovery of ko and As were 54.3% and 65% of its starting materials (DNP-Protein). Sample Ta´s recovery was 85% of its DNP-protein.
λ-type of Bence Jones Protein was rot investigated its N-terminal amino acid residue by DNP-method, probably it was blocked its N-terminal residue with glutamic acid.
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KEYWORD
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