. Author manuscript; available in PMC: 2010 Jun 28.

Published in final edited form as: Top Clin Nutr. 2009 Oct;24(4):359–365. doi: 10.1097/TIN.0b013e3181c62182

Table 1.

Subject Characteristics

			Residual Enzyme Activities (nmol/min/mg protein)
Age (yr)	Gender	Mutations	LCHAD	Thiolase
10.3	M	c.1528G>C/c.1528G>C	11.8	38.6
12.7	F	c.1528G>C/c.1528G>C	10.7	21.0
13.6	M	c.1528G>C/c.1678C>T	NA	NA
8.4	F	c.1528G>C/c.274–278del	10.2	10.7
12.6	M	c.1528G>C/?	NA	NA
14.1	F	c.1528G>C/c.479–482TAGC>AATA	NA	NA
^*8.7	F	c.901G>A β-subunit/?	12.4	0.4
^*14.4	F	c.901G>A β-subunit/?	NA	NA

indicates siblings

Mutations are in the alpha subunit of the trifunctional protein unless otherwise noted. “?” indicated alleles in which no mutations were identified following the sequencing of exons in both the alpha and beta subunits. Patients have one known mutation and clinical and biochemical evidence of LCHAD or TFP deficiency.