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The purification and partial characterization of human salivary kallikrein



The purification and partial characterization of human salivary kallikrein



Biochimica et Biophysica Acta 709(1): 65-72



The major arginine esterase activity in human saliva was purified. This enzyme lowers the blood pressure of a rabbit and produces kinins in acid treated dog plasma. It is therefore a kallikrein. The kallikrein has an unusual amino acid composition: Asp and Glu comprise 40% of the residues; the total number of basic residues is less than 5%; Gly and Pro together make up more than 40% of the residues. The enzyme has a pI of 4.0 and an MW of 27,000 as determined by dodecyl sulfate gel electrophoresis. On the other hand, sedimentation equilibrium data and the amino acid composition give an MW value of only 9600. The enzyme could be a rather asymmetric molecule. The circular dichroism spectrum shows a minimum at 200 nm with [.theta.] = -28,000 deg .cntdot. cm2 .cntdot. dmol-1. The enzyme structure contains polyproline form II helix together with .beta.-turns. This structure is stable in the presence of dodecyl sulfate.

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Accession: 006744513

Download citation: RISBibTeXText

PMID: 6924862

DOI: 10.1016/0167-4838(82)90422-8


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