Tris(hydroxymethyl)aminomethane Buffer and Amino Acid Analysis.

This paper presents a simple and rapid procedure for the isolation of ribulose-l,5-diphosphate carboxylase from leaves. By column chromatography on Sephadex G-25 and Sepharose 6B combined with concentration by ultrafiltration high yields of undenatured protein are obtainable in less than one working day. RudP carboxylase purified from barley in this way has been characterized. The molecular size is similar to that of spinach, wheat and oat. The apparent molecular weight determined by column chromatography was found to be 510,000, approximately 3 % higher than that for the tobacco protein in the same systems. RudP carboxylase from barley consists of two different kinds of subunits with the same molecular weight properties as described for other plants. The amino acid composition of the native protein shows similarities with another monocotyledon, oat, both having lower contents of leucine and tyrosine than the dicotyledons, spinach and tobacco. The high content of tryptophan in barley RudP carboxylase gives a higher extinction at 280 nm than has been reported for other organisms (E 1%o = 2.06). This paper also describes a mapping technique for the tryptic peptides of the su-280 nm bunits of RudP carboxylase by two-dimensional high voltage paper electrophoresis which is rapid, reproducible and gives well defined spots. The peptide mapping technique is well suited as a screening method for RudP carboxylase mutants.

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Tris(hydroxymethyl)aminomethane Buffer and Amino Acid Analysis.

Cited by 2 publications

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ChemInform Abstract: TRIS(HYDROXYMETHYL)AMINOMETHANE (TRIS) BUFFER AND AMINO ACID ANALYSIS

ChemInform Abstract: TRIS(HYDROXYMETHYL)AMINOMETHANE (TRIS) BUFFER AND AMINO ACID ANALYSIS

Ribulose-1,5-diphosphate carboxylase from barley (Hordeum vulgare)

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