Studies on Mold Protease
- 1 March 1970
- journal article
- research article
- Published by Oxford University Press (OUP) in The Journal of Biochemistry
- Vol. 67 (3) , 415-420
- https://doi.org/10.1093/oxfordjournals.jbchem.a129265
Abstract
Some physicochemical properties and amino acid composition of crystalline acid protease [Peptide peptidohydrolase, EC class 3. 4. 4] obtained from Rhizopus chinensis were determined. The s20, w and molecular weight of the enzyme were found by ultra-centrifugal analyses to be 2.83 and 35,000, respectively. The enzyme consisted of single polypeptide chain with alanine as the amino terminus and was composed of 324 residues of amino acids: Lys12, His0, Arg9, Asp43, Thr32, Ser26, Glu21, Pro14, Gly3, Ala23, 1/2Cys4, Val19Phe16, Trp5 and amide-ammonia32. The optical rotatory dispersion parameters were: [α]D=—33, α=—200, b0=0, λc=208 mμ and [m′)227 mμ=–2,100, suggesting the absence of α-helix structure in the molecule.Keywords
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