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 Cancer detection procedure using an acyl carrier protein

Details
Inventors: Bucovaz, Edsel T.; Whybrew, Walter D.;
Assignee: Research Corporation (Lexington, NY)
Primary Examiner: Padgett; Benjamin R.
Assistant Examiner: Moskowitz; M.
Attorney, Agent or Firm: Scully, Scott, Murphy and Presser

A method of detecting cancer in mammals which comprises admixing with a serum sample from said mammal detectably labelled acyl carrier protein and subsequently determining the amount of B-protein-acyl carrier protein complex which is formed.

DETAILED DESCRIPTION OF THE PREFERRED EMBODIMENT The present diagnostic procedure is based upon the finding that proteins contained in blood serum samples from a cancerous host are different from the proteins in serum samples from a non-cancerous host.
The diagnostic procedure disclosed in the U.
S.
Pat.
No.
4,160,817 relied upon the fact the serum samples from cancer resources denatured to detectably different extent than proteins from a non-cancerous resource.
The procedure of our application Ser.
No.
246,311 now U.
S.
Pat.
No.
4,368,262, issued Jan.
11, 1983, was based on the further discovery that the precipitated proteins obtained from a cancer resource resolubilized to detectably different extent than did protein precipitated from non-cancer resources.
The present diagnostic procedure relies upon the same two findings to allow one to discriminate between cancerous and non-cancerous serum samples.
The present diagnostic procedure relies upon the use of a detectably labeled acyl carrier protein for success.
Acyl carrier proteins are found in many substances in nature.
The particular source of acyl carrier protein is not critical and it can be derived from any source such as Escherichia coli B cells or E.
coli K 12 UB 1005 disclosed by Rock et al in Analytical Biochemistry 102, pages 362 to 364 (1980).
An acyl carrier protein-like material has also been identified as being components of the multi-enzyme complex of yeast fatty-acid-synthetase complex.
Any of these sources may be used in the preparation of acyl carrier protein.
The only criteria is that the acyl carrier protein be in active form which promotes fatty acid synthesis from acetyl-CoA and malonyl-CoA in the presence of other required components (Prescott, D.
J.
and Vagelos, P.
R.
, Advances in Enzymology, 31 269 (1972) and conform holo-ACP from apo-ACP and CoA in the presence of phosphopantetheinetransferase.
A particularly preferred technique for preparing acyl carrier protein is that described by Rock et al cited previously



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