Women in Thoracic Surgery was founded in 1986, with 2016 marking its 30th anniversary. Reflecting back on the last 3 decades of history, accomplishments, and enormous strides in our field, we review the past, present, and future of this organization. Although women still constitute a small minority of practicing surgeons in our field today, opportunities currently abound for women in thoracic surgery. Owing much to the early female pioneers in the field and to the support of male sponsors and our national societies, Women in Thoracic Surgery has grown and prospered, as have its members and the global community of female thoracic surgeons as a whole. In celebration of our 30th anniversary, we share with the readership the rich history of Women in Thoracic Surgery and its goals for the future.

Palmitoylcarnitine was oxidised by pea mitochondria.L-carnitine was an essential addition for the oxidation of palmitate or palmitoylCoA. When palmitate was sole substrate, ATP and Mg(2+) were also essential additives for maximum oxidation. Additions of CoA inhibited the oxidation of palmitate. It was shown that CoA was acting as a competitive inhibitor of the carnitine-stimulated O2 uptake. It is suggested that palmitoylacarnitine and carnitine passed through the mitochondrial barrier with ease but palmitoylCoA and CoA did not. The presence of carnitine long-chain acyl (palmitoyl)transferase (EC 2.3.1.21) in pea-cotyledon mitochondria was shown. This enzyme may play a role in the transport of long-chain acyl groups through membrane barriers.

β-Oxidation enzymes were detected both in the mitochondria and microbodies of pea cotyledons. Intact mitochondria did not show β-oxidation enzyme activity but in ruptured mitochondria this activity was high. It is apparent that the mitochondrial membrane barrier prevents rapid access of acyl-CoA substrates to matrix β-oxidation sites. Removal of the membrane barrier permits rapid access of acyl-CoAs and these enzyme activities may then be measured.

Purified pea cotyledon mitochondria did not oxidise acetyl-CoA in the presence of carnitine. However, acetylcarnitine was oxidised. It was concluded that acetylcarnitine passed through the mitochondrial membrane barrier but acetyl-CoA did not. Only a sensitive radioactive assay detected carnitine acetyltransferase in intact mitochondrion or intact mitoplast preparations. When the mitochondria or mitoplasts were burst, acetyl-CoA substrate was available to the matrix carnitine acetyltransferase and a high activity of the enzyme was measured. The inner mitochondrial membrane is there-fore the membrane barrier to acetyl-CoA but acetylcarnitine is suggested to be transported through this membrane via an integral carnitine: acylcarnitine translocator. Evidence is presented to indicate that when the cotyledons from 48-h-grown peas are oxidising pyruvate, acetylcarnitine formed in the mitochondrial matrix by the action of matrix carnitine acetyltransferase may be transported to extra-mitochondrial sites via the membrane translocator.

A method is described for separating mitochondria from microbodies in cotyledon preparations of Pisum sativum L. cv. Alaska. Pure and intact mitochondria were obtained on a continuous: discontinuous sucrose density gradient as shown by marke-enzyme assay and electron microscopy. Manipulation of sucrose-gradient construction to widen the distance between organelles provided a quick method for the separation of the mitochondria from the microbodies. The shorter time of exposure of mitochondria to centrifugation and osmotic stress produces mitochondria free of contamination.