cDNA Cloning, Biological and Immunological Characterization of the Alkaline Serine Protease Major Allergen from Penicillium chrysogenum

2002 ◽  
Vol 127 (1) ◽  
pp. 15-26 ◽  
Author(s):  
Hong Chou ◽  
Hsiu-Yu Lai ◽  
Ming F. Tam ◽  
Ming-Yuan Chou ◽  
Soo-Ray Wang ◽  
...  
Keyword(s):  
Serine Protease ◽  
Cdna Cloning ◽  
Penicillium Chrysogenum ◽  
Major Allergen ◽  
Alkaline Serine Protease ◽  
Immunological Characterization

Molecular and immunological characterization of Pen ch 18, the vacuolar serine protease major allergen of Penicillium chrysogenum

Allergy ◽  
2003 ◽  
Vol 58 (10) ◽  
pp. 993-1002 ◽  
Author(s):  
H.-D. Shen ◽  
H. Chou ◽  
M. F. Tam ◽  
C.-Y. Chang ◽  
H.-Y. Lai ◽  
...  
Keyword(s):  
Serine Protease ◽  
Penicillium Chrysogenum ◽  
Major Allergen ◽  
Immunological Characterization

Molecular and immunological characterization of subtilisin like serine protease, a major allergen of Curvularia lunata

Immunobiology ◽  
2011 ◽  
Vol 216 (3) ◽  
pp. 402-408 ◽  
Author(s):  
Prabhanshu Tripathi ◽  
Smitha Nair ◽  
B.P. Singh ◽  
Naveen Arora
Keyword(s):  
Serine Protease ◽  
Major Allergen ◽  
Curvularia Lunata ◽  
Immunological Characterization

cDNA cloning and immunologic characterization of Pen o 18, the vacuolar serine protease major allergen of Penicillium oxalicum

2001 ◽  
Vol 137 (2) ◽  
pp. 115-124 ◽  
Author(s):  
Horng-Der Shen ◽  
Chih-Wen Wang ◽  
Win-Ling Lin ◽  
Hsiu-Yu Lai ◽  
Ming F. Tam ◽  
...  
Keyword(s):  
Serine Protease ◽  
Cdna Cloning ◽  
Major Allergen ◽  
Penicillium Oxalicum ◽  
O 18

scholarly journals Purification and Biochemical Characterization of Alkaline Serine Protease from Caesalpinia bonducella

2010 ◽  
Vol 5 (6) ◽  
pp. 1934578X1000500
Author(s):  
Hidayatullah Khan ◽  
Irshad Ali ◽  
Arif-ullah Khan ◽  
Mushtaq Ahmed ◽  
Zamarud Shah ◽  
...  
Keyword(s):  
Serine Protease ◽  
Biochemical Characterization ◽  
Specific Activity ◽  
Sodium Dodecyl ◽  
Exchange Chromatography ◽  
Size Exclusion ◽  
Alkaline Serine Protease ◽  
Protease Enzyme ◽  
Caesalpinia Bonducella

A high molecular weight serine protease has been purified to electrophoretic homogeneity from the seeds of Caesalpinia bonducella Flem. (Caesalpiniaceae) by the combination of size exclusion and ion exchange chromatography. About 524 fold purification was achieved with an overall recovery of 6.8%. The specific activity was found to be 86 U/mg/min at pH 8.0. The calculated Km and Vmax were 1.66 mg/mL and 496.68 units/min per mg of protein, respectively. The molecular mass was estimated to be about 63 kDa by sodium dodecyl sulfate PAGE. The enzyme showed optimum activity at pH 8.0 and exhibited its highest activity at 40°C. The enzyme was strongly inhibited by 2mM phenylmethylsulfonyl fluoride (PMSF), suggesting the presence of a serine residue at the active site. PMSF showed a pure competitive type of inhibition with the serine protease enzyme. It was observed that enzyme activity was enhanced in the presence of dications and was active against a variety of modified substrates and natural proteins.

Cloning, expression and immunological characterization of Ory s 1, the major allergen of rice pollen

Gene ◽  
1995 ◽  
Vol 164 (2) ◽  
pp. 255-259 ◽  
Author(s):  
Huiling Xu ◽  
Piyada Theerakulpisut ◽  
Neil Goulding ◽  
Cenk Suphioglu ◽  
Mohan B. Singh ◽  
...  
Keyword(s):  
Major Allergen ◽  
Immunological Characterization
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