In a previous communication from this laboratory (Stockell Hartree, Thomas, Braikevitch, Bell, Christie, Spaull, Taylor & Pierce, 1971) it was reported that the sialic acid contents of the subunits of human luteinizing hormone (LH) were very much less than in the intact hormone. This finding was unexpected since the subunits were still capable of recombination with restoration of full biological activity. The demonstration that marked loss of biological activity occurred in human LH after removal of sialic acid by treatment of the intact hormone with neuraminidase (Braunstein, Reichert, Van Hall, Vaitukaitis & Ross, 1971) has prompted us to reinvestigate the sialic acid contents of the subunits. In addition, the tryptophan content of the subunits has been measured by the spectrophotometric method of Bencze & Schmid (1957).
Estimations were performed on subunits prepared by two different methods. In each case intact LH of potency 3–5 mg NIH-LH-S1/mg (Stockell Hartree, 1966) was
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