scholarly journals The deduced amino acid sequence of human carbonic anhydrase-related protein (CARP) is 98% identical to the mouse homologue

Gene ◽  
1993 ◽  
Vol 126 (2) ◽  
pp. 291-292 ◽  
Author(s):  
Laura A. Skaggs ◽  
Nils C.H. Bergenhem ◽  
Patrick J. Venta ◽  
Richard E. Tashian
2020 ◽  
Vol 35 (1) ◽  
pp. 489-497 ◽  
Author(s):  
Hasan Küçükbay ◽  
Nesrin Buğday ◽  
F. Zehra Küçükbay ◽  
Andrea Ageli ◽  
Gianluca Bartolucci ◽  
...  

1978 ◽  
Vol 533 (1) ◽  
pp. 1-11 ◽  
Author(s):  
Robert E. Ferrell ◽  
Sharon K. Stroup ◽  
Robert J. Tanis ◽  
Richard E. Tashian

2009 ◽  
Vol 76 (2) ◽  
pp. 507-511 ◽  
Author(s):  
Sarah S. Picaud ◽  
João R. C. Muniz ◽  
Anneke Kramm ◽  
Ewa S. Pilka ◽  
Grazyna Kochan ◽  
...  

1970 ◽  
Vol 14 ◽  
pp. 1-9
Author(s):  
Mohammad Taufiq Alam

In both, bovine and human carbonic anhydrase II, a conserved glutamine residue occupies the position in the middle of the knot, which is formed by intercrossing of C-terminal end with N-terminal region. Previous studies have indicated that C-terminus is not the part of an active site, but truncation of 7 amino acid residue in this region can have marked effects on stability of the enzyme (data not published). To gain further insight into the role of specific amino acid residue in C-terminal region, site directed mutagenesis was used to introduce point mutation. Substitution of glutamine with cysteine was chosen because the cysteine residue is less hydrophilic as compared with glutamine and thus, may disrupt the hydrophilic environment in this region. Result indicates that Gln253 located within the C-terminus knot topology plays a significant role in normal function of the enzyme. Thus, C-terminal region might mediate cooperativity between the central active site of the enzyme through proper formation of knot. Key words: Human carbonic anhydrase II; knot topology; point mutation J. bio-sci. 14: 1-9, 2006


1993 ◽  
Vol 106 (1) ◽  
pp. 401-409 ◽  
Author(s):  
H. Matsunami ◽  
S. Miyatani ◽  
T. Inoue ◽  
N.G. Copeland ◽  
D.J. Gilbert ◽  
...  

R-cadherin was originally identified as a chicken cadherin expressed by the retina. Here, we describe the identification of a mouse homologue of R-cadherin. We isolated mouse cDNAs encoding a cadherin with 94% identity in amino acid sequence to the chicken R-cadherin, and defined this molecule as mouse R-cadherin. L cells transfected with the mouse R-cadherin cDNA acquired a cadherin-mediated cell-cell adhesiveness as found for other cadherins. To examine the binding specificity of mouse R-cadherin, L cells expressing this cadherin (mRL) were mixed with L cells expressing chicken R-cadherin (cRL), mouse N-cadherin (mNL), mouse E-cadherin (mEL) and mouse P-cadherin (mPL). While mRL cells randomly intermixed with cRL cells, those cells aggregated separately from mEL or mPL cells. Mixing of mRL with mNL cells gave an intermediate result; that is, they formed both separate and chimeric aggregates, suggesting that R- and N-cadherin can interact with each other although each has a preference to bind to its own type. Similar properties were previously found for chicken R-cadherin. Thus, the cell binding specificity of R-cadherin is entirely conserved between the two species, suggesting a conserved role for this protein in morphogenesis. We also located the mouse R-cadherin gene to chromosome 2.


Gene ◽  
1986 ◽  
Vol 41 (2-3) ◽  
pp. 233-239 ◽  
Author(s):  
Julie Lloyd ◽  
Sheila McMillan ◽  
David Hopkinson ◽  
Yvonne H. Edwards

Biochemistry ◽  
1988 ◽  
Vol 27 (8) ◽  
pp. 2815-2820 ◽  
Author(s):  
Ross T. Fernley ◽  
R. Douglas Wright ◽  
John P. Coghlan

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