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The myoglobin of primates. VIII. Nycticebus coucang (slow loris)
Biochimica Et Biophysica Acta
|February 20, 1976
Abstract:
To the analysis of three prosimian myoglobins reported previously [1, 2] that of the slow loris (Nycticebus coucang) has been added. A cladogram has been constructed utilising the new information to arrive at a possible ancestral prosimian myoglobin. Within the primates only the four prosimians share residues of threonine at position 34 and of isoleucine at position 142. During tryptic digestion of the loris myoglobin, some hydrolysis was observed at bonds not usually considered to be susceptible to the action of this enzyme: 52 Pro-53 Asp, and 120 Pro-121 Gly.