cDNA cloning, expression, and enzymatic activity of a novel endogenous cellulase from the beetle Batocera horsfieldi

Gene ◽  
2013 ◽  
Vol 514 (1) ◽  
pp. 62-68 ◽  
Author(s):  
Dingguo Xia ◽  
Yadong Wei ◽  
Guozheng Zhang ◽  
Qiaoling Zhao ◽  
Yeshun Zhang ◽  
...  
Keyword(s):  
Enzymatic Activity ◽  
Cdna Cloning ◽  
Batocera Horsfieldi

A novel plant peptidyl-prolyl-cis-trans-isomerase (PPIase): cDNA cloning, structural analysis, enzymatic activity and expression

1996 ◽  
Vol 32 (3) ◽  
pp. 493-504 ◽  
Author(s):  
Oshra Blecher ◽  
Noa Erel ◽  
Isabelle Callebaut ◽  
Keren Aviezer ◽  
Adina Breiman
Keyword(s):  
Structural Analysis ◽  
Enzymatic Activity ◽  
Cdna Cloning

cDNA cloning, expression, and enzymatic activity of a cellulase from the mulberry longicorn beetle, Apriona germari

2004 ◽  
Vol 139 (1) ◽  
pp. 107-116 ◽  
Author(s):  
Seong Jin Lee ◽  
Seong Ryul Kim ◽  
Hyung Joo Yoon ◽  
Iksoo Kim ◽  
Kwang Sik Lee ◽  
...  
Keyword(s):  
Enzymatic Activity ◽  
Cdna Cloning ◽  
Longicorn Beetle

scholarly journals A gut-specific chitinase from the mulberry longicorn beetle, Apriona germari (Coleoptera: Cerambycidae): cDNA cloning, gene structure, expression and enzymatic activity

2007 ◽  
Vol 104 (2) ◽  
pp. 173-180 ◽  
Author(s):  
Young Moo CHOO ◽  
Kwang Sik LEE ◽  
Bo Yeon KIM ◽  
Doh Hoon KIM ◽  
Hyung Joo YOON ◽  
...  
Keyword(s):  
Enzymatic Activity ◽  
Cdna Cloning ◽  
Gene Structure ◽  
Longicorn Beetle

cDNA cloning and expression of a gamma-aminobutyric acidA receptor epsilon-subunit in rat brain

2000 ◽  
Vol 12 (12) ◽  
pp. 4318-4330 ◽  
Author(s):  
Nathalie Moragues ◽  
Philippe Ciofi ◽  
Pierrette Lafon ◽  
Marie-Francoise Odessa ◽  
Gerard Tramu ◽  
...  
Keyword(s):  
Rat Brain ◽  
Cdna Cloning ◽  
Cloning And Expression ◽  
Epsilon Subunit

A Method for the Colorimetric Determination of β-Glucuronidase in Urine, Serum, Tissue; Assay of Enzymatic Activity in Health and Disease

1959 ◽  
Vol 36 (2) ◽  
pp. 193-201 ◽  
Author(s):  
Julius A. Goldbarg ◽  
Esteban P. Pineda ◽  
Benjamin M. Banks ◽  
Alexander M. Rutenburg
Keyword(s):  
Enzymatic Activity ◽  
Colorimetric Determination ◽  
Health And Disease ◽  
Urine Serum

Murine CD70: cDNA cloning and gene structure

1997 ◽  
Vol 56 (1-3) ◽  
pp. 56
Author(s):  
K Tesselaar
Keyword(s):  
Cdna Cloning ◽  
Gene Structure

Isolation of Antithrombin III from Normal and α1-Antitrypsin-Deficient Human Plasma

1977 ◽  
Vol 38 (02) ◽  
pp. 0475-0485 ◽  
Author(s):  
Anna D. Borsodi ◽  
Ralph A. Bradshaw
Keyword(s):  
Enzymatic Activity ◽  
Isoelectric Focusing ◽  
Antithrombin Iii ◽  
Factor Xa ◽  
Antithrombin Activity ◽  
Bovine Trypsin ◽  
Normal Plasma ◽  
Antitrypsin Deficiency ◽  
Simplified Procedure ◽  
Stimulation Of

SummaryThe plasma of individuals, hetero- or homozygous for α1-antitrypsin deficiency, contains greatly decreased amounts of antithrombin activity as assayed against factor Xa. However, heparin stimulation of the residual antithrombin activity is observed, which is comparable to that of normal plasma. Antithrombins isolated from both normal and α1-antitrypsin deficient plasma by a simplified procedure are indistinguishable in both properties and yields. The microheterogeneity observed on isoelectric focusing of both preparations can be eliminated by treatment with neuraminidase. Neither purified human antithrombin nor α1-antitrypsin, when assayed against bovine trypsin, is stimulated by heparin. These results clearly establish the unique natures of antithrombin and α1-antitrypsin and show that about 75% of the antithrombin activity measured in normal plasma is due to α1-antitrypsin. Estimates of anti thrombin III activity in normal plasma by assays dependent on enzymatic activity can probably be obtained only in the presence of heparin.

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