Immunoreactivities of p11 and calcyclin in baker's yeast, wheat germ and lobster.
After effectively eliminating the nonspecific cross-immunoreactivity with the affinity columns of anti-IgG agarose and IgG agarose, the potent immunoreactivities of p11 and calcyclin in wheat germ, lobster tail muscle, and three strains of baker's yeast were analyzed by Western blotting using mouse anti-p11 and rabbit anti-calcyclin. The occurrence of multiple bands may be due to either autolyses and/or the interactions between the p11 (or calcyclin) and other endogenous biological molecules. The results suggest not only a ubiquitous distribution and a universal Ca(2+)-mediating regulatory role of p11 and calcyclin in eukaryotes, but also an evolutionary conservation of these (S-100)-related proteins.
Kuo
W N
WN
Division of Science and Mathematics, Bethune-Cookman College, Daytona Beach, Florida 32115, USA.
Jn-Baptiste
J B
JB
Zhai
L
L
Chambers
M C
MC
Kanadia
R
R
D000818:Animals; D017302:Annexins / Q000032:analysis* / Q000276:immunology; D015153:Blotting, Western; D002135:Calcium-Binding Proteins / Q000032:analysis* / Q000276:immunology; D018797:Cell Cycle Proteins; D008121:Nephropidae / Q000737:chemistry*; D000075383:S100 Calcium Binding Protein A6; D009418:S100 Proteins; D012441:Saccharomyces cerevisiae / Q000737:chemistry*; D014908:Triticum / Q000737:chemistry*
D017302:Annexins; D002135:Calcium-Binding Proteins; D018797:Cell Cycle Proteins; D000075383:S100 Calcium Binding Protein A6; D009418:S100 Proteins; C489134:S100a6 protein, mouse