Literature DB >> 7019156

Physico-chemical properties of the acid proteinase from A. fumigatus.

M Panneerselvam, S C Dhar.   

Abstract

The physico-chemical properties of the purified acid proteinase were investigated. This enzyme was found to hydrolyze hemoglobin maximally among the different substrates used. The maximum hydrolysis of hemoglobin was found at pH 2.8 and 45 degrees C in 30 min. Km value of 5.5 X 10(-4) M was obtained from the Lineweaver Burk plot for the hydrolysis of hemoglobin. The enzyme was found to be most stable at pH 4.9. The maximum stability of the enzyme was observed with 2 per cent casein as a stabilising agent. It was found to have a molecular weight 37,500 consisting of 298 aminoacid residues. The partial specific volume of the acid proteinase was found to be 0.734 ml/g. Leucine and alanine were the amino and carboxy terminal aminoacids of the acid proteinase respectively.

Entities:  

Mesh:

Substances:

Year:  1981        PMID: 7019156

Source DB:  PubMed          Journal:  Ital J Biochem        ISSN: 0021-2938


  2 in total

1.  Purification and characterization of an elastinolytic metalloprotease from Aspergillus fumigatus and immunoelectron microscopic evidence of secretion of this enzyme by the fungus invading the murine lung.

Authors:  A Markaryan; I Morozova; H Yu; P E Kolattukudy
Journal:  Infect Immun       Date:  1994-06       Impact factor: 3.441

2.  Isolation and characterization of a secreted metalloprotease of Aspergillus fumigatus.

Authors:  M Monod; S Paris; D Sanglard; K Jaton-Ogay; J Bille; J P Latgé
Journal:  Infect Immun       Date:  1993-10       Impact factor: 3.441

  2 in total

北京卡尤迪生物科技股份有限公司 © 2022-2023.