Antigenic and Biochemical Characterization of Poliovirus Type 2 Isolated from Two Cases of Paralytic Disease

Intervirology ◽  
1987 ◽  
Vol 27 (4) ◽  
pp. 196-204 ◽  
Author(s):  
Lucia Fiore ◽  
Alessandra Pierangeli ◽  
Franco Lombard ◽  
Regina Santoro ◽  
Radu Crainic ◽  
...  
Keyword(s):  
Biochemical Characterization ◽  
Poliovirus Type

Biochemical characterization of poliovirus type 1 temperature-sensitive mutants

Virology ◽  
1984 ◽  
Vol 139 (2) ◽  
pp. 403-407 ◽  
Author(s):  
Christine Bellocq ◽  
Henri Agut ◽  
Sylvie Van Der Werf ◽  
Marc Girard
Keyword(s):  
Biochemical Characterization ◽  
Temperature Sensitive ◽  
Poliovirus Type ◽  
Temperature Sensitive Mutants

Antigenic and Biochemical Characterization of Poliovirus Type 1 Isolates

1987 ◽  
Vol 31 (4) ◽  
pp. 327-336 ◽  
Author(s):  
Minoru Hara ◽  
Mineo Arita ◽  
Zenichi Yamazaki ◽  
Akio Hagiwara ◽  
Yoshiko Saito
Keyword(s):  
Biochemical Characterization ◽  
Poliovirus Type

Biochemical Characterization of a Monoclonal Antibody to the H Type-2 Antigen: Comparison to Other ABH Antibodies

Hybridoma ◽  
1986 ◽  
Vol 5 (2) ◽  
pp. 117-127 ◽  
Author(s):  
BARNETT B. ROSENBLUM ◽  
W. JOHN JUDD ◽  
THOMAS E. CAREY
Keyword(s):  
Monoclonal Antibody ◽  
Biochemical Characterization

scholarly journals Molecular biological and biochemical characterization of the human type 2 selenodeiodinase.

Endocrinology ◽  
1996 ◽  
Vol 137 (8) ◽  
pp. 3308-3315 ◽  
Author(s):  
D Salvatore ◽  
T Bartha ◽  
J W Harney ◽  
P R Larsen
Keyword(s):  
Biochemical Characterization ◽  
Human Type

scholarly journals Biochemical Characterization of Bovine Brain Myristoyl-CoA:Protein N-Myristoyltransferase Type 2

2009 ◽  
Vol 2009 ◽  
pp. 1-9 ◽  
Author(s):  
Ponniah Selvakumar ◽  
Ashakumary Lakshmikuttyamma ◽  
Rajendra K. Sharma
Keyword(s):  
Metal Ion ◽  
Biochemical Characterization ◽  
Kinetic Studies ◽  
Bovine Brain ◽  
Covalent Attachment ◽  
Reading Frame ◽  
Gene Coding ◽  
Acid Protein

Protein N-myristoylation is a lipidic modification which refers to the covalent attachment of myristate, a 14-carbon saturated fatty acid, to the N-terminal glycine residue of a number of mammalian, viral, and fungal proteins. In this paper, we have cloned the gene coding for myristoyl-CoA:protein N-myristoyltransferase (NMT) fromBos tarusbrain. The open reading frame codes for a 410-amino-acid protein and overexpressed inEscherichia coli. Kinetic studies suggested that bovine brain NMT2 and human NMT1 show significant differences in their peptide substrate specificities. The metal ionCa2+had stimulatory effects on NMT2 activity whileMn2+andZn2+inhibited the enzyme activity. In addition, NMT2 activity was inhibited by various organic solvents and other detergents while NMT1 had a stimulatory effect. Biochemical characterization suggested that both forms of NMT have unique characteristics. Further analysis towards functional role NMT2 will lead the development of therapeutic target for the progression of various diseases such as cancer, cardiovascular diseases, and neurodegenerative diseases.

scholarly journals Production and Characterization of a Monoclonal Antibody Neutralizing Poliovirus Type 2

2019 ◽  
Author(s):  
Morteza Kamalzadeh ◽  
Sina Soleimani ◽  
Mohsen Lotfi
Keyword(s):  
Public Health ◽  
High Specificity ◽  
Cross Reactivity ◽  
Poliovirus Type ◽  
Kappa Chain ◽  
Antibody Assays ◽  
And Control ◽  
Limiting Dilution

Monoclonal Antibodies (mAbs) are used for biomedical research, diagnosis, treatment, production, and the quality control of biological products. mAbs are also very helpful in poliovirus research studies because it is still one of the major public health problems in developing countries. The main objective of this study was the production of mAbs against Poliovirus Type 2 (PV2) to be prepared and respond to the re-emergence of this virus. After fusion of immunized B cells prepared from mice with myeloma tumor cells and screening of about 250 hybridoma colonies, 22 with the highest antibody titer and without cross-reaction with others types were selected and cloned by limiting dilution. In the end, two colonies capable of secreting mAbs against epitopes of PV2 were used to produce mAbs. The mAbs were characterized by antibody assays, isotyping, and epitopes analysis using western blotting test, the crossreactivity with other types, as well as stability, sterility, and mycoplasma tests. The results indicated that the produced mAbs had high specificity, sensitivity and stability against PV2 without any cross-reactivity and were of IgG1 Kappa chain with similar bands at 26 kDa during electrophoresis associated with viral protein VP3 neutralization. These mAbs were specific in serum neutralization tests for PV2 vaccine strain, and therefore, they are potentially valuable for routine polio research, diagnosis, isolation, production, and control of poliovirus vaccines.

scholarly journals The Mammalian Cytosolic Type 2 (R)-β-hydroxybutyrate Dehydrogenase (BDH2) is 4-oxo-L-proline Reductase (EC 1.1.1.104)

2021 ◽  
Author(s):  
Sebastian P. Kwiatkowski ◽  
Maria Bozko ◽  
Michal Zarod ◽  
Apolonia Witecka ◽  
Adam K. Jagielski ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Biochemical Characterization ◽  
Mass Spectrometry Analysis ◽  
Protein Preparation ◽  
Spectrometry Analysis ◽  
E Coli ◽  
Mammalian Tissues ◽  
Reversible Reduction

AbstractThe early studies on chicken embryos revealed that exposition to 4-oxo-L-proline resulted in the explicit increase in 4-hydroxy-L-proline content in their tissues. In 1962, 4-oxo-L-proline reductase, an enzyme responsible for the reduction of 4-oxo-L-proline, was partially purified from rabbit kidneys and characterized biochemically, but only recently the molecular identity of the enzyme has been unveiled in our laboratory. The present investigation reports the purification, identification as well as biochemical characterization of 4-oxo-L-proline reductase. The enzyme was purified from rat kidneys about 280-fold. Following mass spectrometry analysis of the purified protein preparation, the mammalian cytosolic type 2 (R)-β-hydroxybutyrate dehydrogenase (BDH2) emerged as the only meaningful candidate for the reductase. Rat and human BDH2 were expressed in E. coli, purified, and shown to catalyze the reversible reduction of 4-oxo-L-proline to cis-4-hydroxy-L-proline, as confirmed by chromatographic and mass spectrometry analysis. Specificity studies carried out on both enzymes showed that 4-oxo-L-proline was the best substrate, particularly the human enzyme acted with 9400-fold higher catalytic efficiencies on 4-oxo-L-proline than on (R)-β-hydroxybutyrate. Finally, HEK293T cells efficiently metabolized 4-oxo-L-proline to cis-4-hydroxy-L-proline and simultaneously accumulated trans-4-hydroxy-L-proline in the culture medium, suggesting that 4-oxo-L-proline is most likely an inhibitor of trans-4-hydroxy-L-proline metabolism in human cells. We conclude that BDH2 is mammalian 4-oxo-L-proline reductase that converts 4-oxo-L-proline to cis-4-hydroxy-L-proline, and not to trans-4-hydroxy-L-proline as currently thought, and hypothesize that the enzyme may be considered as a potential source of cis-4-hydroxy-L-proline in mammalian tissues.

Antigenic and Biochemical Characterization of Poliovirus Type 1 Isolates of Non-Vaccine Origin

1983 ◽  
Vol 27 (12) ◽  
pp. 1057-1065 ◽  
Author(s):  
Minora Hara ◽  
Akio Hagiwara ◽  
Tetsuo Yoneyama ◽  
Yoshiko Saito ◽  
Hiroto Shimojo
Keyword(s):  
Biochemical Characterization ◽  
Poliovirus Type
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