The world's first wiki where authorship really matters (Nature Genetics, 2008). Due credit and reputation for authors. Imagine a global collaborative knowledge base for original thoughts. Search thousands of articles and collaborate with scientists around the globe.

wikigene or wiki gene protein drug chemical gene disease author authorship tracking collaborative publishing evolutionary knowledge reputation system wiki2.0 global collaboration genes proteins drugs chemicals diseases compound
Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)

Cloning and sequence of multiple forms of phospholipase C.

Three phospholipase C isozymes (PLC-I, II, and III) have been purified from bovine brain. Here, phospholipase C-related cDNA clones corresponding to PLC-I and PLC-III were isolated from a rat brain lambda gt11 expression cDNA library using specific monoclonal antibodies and sequenced. Each of them encodes a distinct polypeptide with a calculated molecular mass of 138,225 (PLC-I) and 85,840 ( PLC-III). Comparison of these two with the sequence of another isozyme PLC-II (Mr = 148,431) that we have previously characterized revealed a low overall sequence homology. Nevertheless, a significant amino acid sequence similarity between the three enzymes was found in two regions, one of about 150 amino acids and the other of about 120 amino acids. The two conserved domains were separated by a variable region. The variable region sequence of PLC-II is relatively long and has recently been shown to contain regions homologous to the noncatalytic domain of the nonreceptor tyrosine kinases. Those of PLC-I and III were short and appeared to be unrelated to these tyrosine kinases. The physiological implications of the multiple species of PLC enzymes are discussed.[1]


  1. Cloning and sequence of multiple forms of phospholipase C. Suh, P.G., Ryu, S.H., Moon, K.H., Suh, H.W., Rhee, S.G. Cell (1988) [Pubmed]
WikiGenes - Universities