The membrane structural lipids of somatic cells and gonidia isolated from Volvox carteri f. nagariensis spheroids have been characterized. The principal polar lipid components of both cell types are sulfoquinovosyl diglyceride, mono-and digalactosyl diglyceride, phosphatidylglycerol, phosphatidylethanolamine, and 1(3), 2-diacylglyceryl-(3)- O--(N,N,N,-tri- Growth was monitored by filtering 1-ml aliquots ofcell suspension through a 4.5-cm-diameter Millipore gridded filter (No. HAWG04700) and counting the spheroids under a dissecting microscope.Harvest and Disruption of Spheroids. Cultures were harvested by pouring the spheroid-containing medium through a No. HC3-90 nylon mesh screen (Tetko, Inc., Elmsford, N. Y.) having a pore size of 90 um. The concentrated spheroids were washed and resuspended in deionized H20 if intended for lipid extraction.If gonidia and somatic cells were to be isolated, approximately 2 x 105 spheroids in stage 1 of development (see legend of Fig. 2), as determined by phase microscopy, were washed and resuspended in 100 ml cold 0.25 M sucrose in 50 mM Tris (pH 7.4). The suspension was then disrupted in the semimicro chamber of a Waring Blendor, model No. 1120, for 30 s at full power. This treatment released intact gonidia from 85-90%/o of the spheroids.The gonidia and somatic cells (many still embedded in fragments of broken spheroid matrix) were separated from any remaining whole spheroids by passage through the 90-,um pore size nylon screen and concentrated by centrifugation at 365g for 5 min. The pellets were resuspended in 35 ml of the disruption buffer, and 5 ml were loaded onto each of seven discontinuous gradients of sucrose in 50 mM Tris (pH 7.4). Each gradient was composed of 5 ml 0.34 M sucrose, 10 ml 1.0 M sucrose, 10 ml 1.46 M sucrose, and 10 ml 2.0 M sucrose. Centrifugation of the loaded gradients for 10 min at 365g produced three bands of green material. Layer 1, located on top of the 1.0 M sucrose, consisted of large sheets of somatic cells embedded in matrix material. Layer 2, located on top of the 1.46 M sucrose, was composed of single somatic cells and small sheets of matrix containing somatic cells. Layer 3, lying above the 2.0 M sucrose, consisted of gonidia, contaminated by a very occasional large sheet of somatic cellcontaining matrix. The purity of the isolated fractions is illustrated in Figure 1.Lipid Extraction and Analysis. Spheroids or isolated cell types were resuspended in a minimum volume ofwater or cell disruption medium, and lipids were extracted by the procedure of Bligh and Dyer (4). Water-soluble impurities were removed by washing the organic phase with a simulated Folch upper phase (10).When a further resolution of the bulk lipid mixture was desired, the washed lipid extract was chromatographed on silicic acid (100 mesh, Mallinckrodt), eluting NL with CHC13, glycolipids with acetone, and PL with CHCl3-methanol (1:1, v/v). TLC of polar lipids was performed, except where noted, on Silica Gel G plates, using the solvent system CHC13-acetic acid-meth...

Fifteen patients with or suspected of having ovarian carcinoma were injected intravenously (i.v.) or intraperitoneally (i.p+) with t3tl-labelled OC 125 F(ab')z. Radioimmunoscintigraphy after i.v. injection revealed 50% of the tumor sites. After i.p. injection all tumor sites were visualized, except in one case in which the antibody remained loculated because of adhesions. One patient with endometrial cancer showed no specific uptake of the antibody after i.p. injection. The serum half-life of the radiolabelled antibody after i.v. injection was 30 hr. After i.p. injection there was a slow appearance of radiolabelled antibody in the blood with a maximum level of 1.4% dose per liter at 24 hr after injection. Urinary excretion of the radiolabel was the same for both routes of administration, with 50% of the dose excreted in approximately 48 hr. Tumor uptake was slightly higher after i.p. injection. Liver and bone marrow uptake after i.p. injection were one-half of the uptake after i.v. injection.Many epithelial ovarian cancers express tumor associated antigens which can be used as targets for imaging (Epenetos et al., 1982; Granowska et al., 1984) or therapy (Epenetos et al., 1986~). One of these markers, CA125, is expressed in more than 80% of these tumors (Kabawat et al., 1983). The antigen can be detected in the serum of ovarian carcinoma patients using a radioimmunometric assay and monoclonal antibody (MAb) OC 125 . A study was undertaken in which patients previously diagnosed with or suspected of having ovarian cancer were injected either intravenously or intraperitoneally with 1311-labelled F(ab')2 fragments of MAb OC125. Patients were scanned at different time intervals after injection. Blood and urine samples were used for pharmacokinetic studies and biopsy specimens were compared for the expression of OC125 antigen and uptake of antibody. PATIENTS AND METHODS PatientsFifteen patients with either a pelvic mass suspected to be ovarian cancer or a confirmed tissue diagnosis of ovarian cancer were entered in this study after informed consent was obtained. Most patients had a laparotomy scheduled 1-7 days after injection of the antibody. MAb OC125 was purified and F(ab')z fragments were prepared. The antibody was radioiodinated to a specific activity of approximately 2.5 mCi I3lI/mg protein (NEN, Boston, MA) (Haisma et al., 1986). The radiolabelled antibody preparation was proven to be apyrogenic and sterile. Immunoreactivity was determined (Lindmo et al., 1984) and found over 80% in all cases. AdministrationPatients received potassium iodide (SSKI, Upsher-Smith, Minneapolis, MN) 48 hr prior to and continuing for 4 days after injection of the antibody. The antibody dose ranged from 0.4 to 8.4 mg protein and the dose of 1311 ranged from 0.7 to 2.7 mCi. For intravenous injection the radiolabelled antibody was administered via a peripheral vein. Intraperitoneal injection was accomplished by diluting the antibody in 500 ml 0.9% saline solution and infusing the solution of antibody through an intra-abdominal catheter ...

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