scholarly journals A structural and functional analysis of the docking protein. Characterization of active domains by proteolysis and specific antibodies.

1985 ◽  
Vol 260 (16) ◽  
pp. 9137-9145
Author(s):  
M Hortsch ◽  
D Avossa ◽  
D I Meyer
Keyword(s):  
Functional Analysis ◽  
Protein Characterization ◽  
Specific Antibodies ◽  
Docking Protein

scholarly journals Characterization of SARS-CoV-2-specific antibodies in COVID-19 patients reveals highly potent neutralizing IgA

2021 ◽  
Vol 6 (1) ◽  
Author(s):  
Weihong Zeng ◽  
Huan Ma ◽  
Chengchao Ding ◽  
Yunru Yang ◽  
Yong Sun ◽  
...  
Keyword(s):  
Specific Antibodies

scholarly journals Odorant-binding protein. Characterization of ligand binding.

1990 ◽  
Vol 265 (11) ◽  
pp. 6118-6125
Author(s):  
J Pevsner ◽  
V Hou ◽  
A M Snowman ◽  
S H Snyder
Keyword(s):  
Ligand Binding ◽  
Binding Protein ◽  
Protein Characterization ◽  
Odorant Binding Protein ◽  
Odorant Binding

Characterization of human type II procollagen and collagen-specific antibodies and their application to the study of human type II collagen processing and ultrastructure

1997 ◽  
Vol 16 (1) ◽  
pp. 29-39 ◽  
Author(s):  
Sergio A. Jimenez ◽  
Leena Ala-Kokko ◽  
Darwin J. Prockop ◽  
Carmen F. Merryman ◽  
Nora Shepard ◽  
...  
Keyword(s):  
Type Ii Collagen ◽  
Type Ii ◽  
Specific Antibodies ◽  
Human Type

scholarly journals Characterization of Glycoside Hydrolase Family 5 Proteins in Schizosaccharomyces pombe

2010 ◽  
Vol 9 (11) ◽  
pp. 1650-1660 ◽  
Author(s):  
Encarnación Dueñas-Santero ◽  
Ana Belén Martín-Cuadrado ◽  
Thierry Fontaine ◽  
Jean-Paul Latgé ◽  
Francisco del Rey ◽  
...  
Keyword(s):  
Cell Wall ◽  
Schizosaccharomyces Pombe ◽  
Protein Characterization ◽  
Wall Material ◽  
Glycoside Hydrolase Family ◽  
Content Type ◽  
Hydrolysis Of ◽  
Controlled Hydrolysis ◽  
Hydrolase Family

ABSTRACT In yeast, enzymes with β-glucanase activity are thought to be necessary in morphogenetic events that require controlled hydrolysis of the cell wall. Comparison of the sequence of the Saccharomyces cerevisiae exo-β(1,3)-glucanase Exg1 with the Schizosaccharomyces pombe genome allowed the identification of three genes that were named exg1 + (locus SPBC1105.05), exg2 + (SPAC12B10.11), and exg3 + (SPBC2D10.05). The three proteins have different localizations: Exg1 is secreted to the periplasmic space, Exg2 is a membrane protein, and Exg3 is a cytoplasmic protein. Characterization of the biochemical activity of the proteins indicated that Exg1 and Exg3 are active only against β(1,6)-glucans while no activity was detected for Exg2. Interestingly, Exg1 cleaves the glucans with an endohydrolytic mode of action. exg1 + showed periodic expression during the cell cycle, with a maximum coinciding with the septation process, and its expression was dependent on the transcription factor Sep1. The Exg1 protein localizes to the septum region in a pattern that was different from that of the endo-β(1,3)-glucanase Eng1. Overexpression of Exg2 resulted in an increase in cell wall material at the poles and in the septum, but the putative catalytic activity of the protein was not required for this effect.

Anti-Peptide Specific Antibodies for the Characterization of Different α Subunits of α-Bungarotoxin Binding Acetylcholine Receptors Present in Chick Optic Lobe

1993 ◽  
Vol 13 (1-4) ◽  
pp. 453-465 ◽  
Author(s):  
Cecilia Gotti ◽  
Milena Moretti ◽  
Renato Longhi ◽  
Luca Briscini ◽  
Ernesto Manera ◽  
...  
Keyword(s):  
Acetylcholine Receptors ◽  
Optic Lobe ◽  
Specific Antibodies ◽  
Chick Optic Lobe ◽  
Α Subunits

scholarly journals Genomic, Tissue Expression, and Protein Characterization of pCLCA1, a Putative Modulator of Cystic Fibrosis in the Pig

2009 ◽  
Vol 57 (12) ◽  
pp. 1169-1181 ◽  
Author(s):  
Stephanie Plog ◽  
Lars Mundhenk ◽  
Nikolai Klymiuk ◽  
Achim D. Gruber
Keyword(s):  
Cystic Fibrosis ◽  
Tissue Expression ◽  
Protein Characterization

scholarly journals Optimization of Expression Condition, Two Dimensional And Melting Point-Based Characterization of Recombinant Human Interferon Alpha-2a Fusion and Non Fusion Forms

2018 ◽  
Vol 22 (2) ◽  
pp. 57
Author(s):  
Ratih Asmana Ningrum ◽  
Widdya Kusuma Wardhani ◽  
Ike Wahyuni ◽  
Apon Zaenal Mustopa
Keyword(s):  
Interferon Alpha ◽  
Protein Characterization ◽  
Protein Yield ◽  
Size Exclusion ◽  
Human Interferon ◽  
Two Dimensional ◽  
Cancer Treatments ◽  
Sds Page ◽  
Bca Assay

     Recombinant Human Interferon Alpha-2a (rhIFNα-2a) is a therapeutic protein that used in hepatitis and cancer treatments. In our previous research, we developed higher molecular weight of the protein through human serum albumin fusion. The fusion and non fusion form of rhIFNα-2a were produced in Pichia pastoriswith 86 kDa and 19 kDa in size respectively. In previous research, protein yield was not reproducible due to unoptimized expression conditions. This reseach was aimed to optimize expression condition process and to characterize the fusion and non fusion forms of rhIFNα-2a. The parameters to observe in overproduction include nutrient (media and methanol concentration) and non nutrient (temperature andincubation period). Affinity and size exclusion cromatographicwere compared in protein purification. BCA assay was used to determine quantity of protein. Protein characterization was conducted using two-dimensional SDS PAGE and denaturation analyses. The optimal condition of expression was achieved using complex media with 1% of methanol for 3 day incubation period at 25°C. The protein yield was reproducible and higher comparing to previous research. Affinity chromatography resulted in higher purity of the proteins comparing to size exclusions. Characterization using two dimensional gel analysis revealed that isoelectric point of rhIFNα-2a is 6.5 for fusion form and 6.0 for non fusion form. The melting points of fusion protein were 56°C and 62°C whilst that of non fusion was 56°C.

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