sodium-dodecyl-sulfate and Neoplasms

For the clinical development of low-dose metronomic (LDM) chemotherapy of paclitaxel, oral administration is vital. However, the development of an oral formulation is difficult due to paclitaxel's low oral bioavailability, caused by its low permeability and low solubility. We increased the oral bioavailability of paclitaxel by combining a pharmacokinetic booster, ritonavir, with a new oral solid dispersion formulation of paclitaxel. The combined use of Hansen solubility parameters and dissolution experiments resulted in the development of a solid dispersion formulation containing 1/11 w/w paclitaxel, 9/11 w/w polyvinylpyrrolidone (PVP) K30, and 1/11 w/w sodium lauryl sulfate (SLS). Analysis of the solid dispersion formulation by X-ray diffraction, Fourier transform infrared (FT-IR) spectroscopy, and modulated differential scanning calorimetry (mDSC) confirmed the amorphous nature of paclitaxel and the fine dispersion of paclitaxel in the matrix of PVP-K30 and SLS. Furthermore, in vitro tests showed a major increase in the apparent solubility and dissolution rate of paclitaxel. To test the clinical significance of these findings, the solid dispersion formulation of paclitaxel (ModraPac001 10mg capsule) was compared to the paclitaxel premix solution in four patients with advanced cancer. Although the mean systemic exposure to paclitaxel after oral administration of the solid dispersion formulation was slightly lower compared to the paclitaxel premix solution (190±63.1ng/mLh for vs. 247±100ng/mLh), the systemic exposure to paclitaxel is clinically relevant [1,2]. In addition to this, the favorable pharmaceutical characteristics, for example, neutral taste, dosing accuracy, and the 2-year ambient shelf life, make the ModraPac001 10mg capsule an attractive candidate for oral paclitaxel chemotherapy. Currently, the ModraPac001 formulation is applied in the first clinical trial with oral LDM chemotherapy of paclitaxel.

Topics: Administration, Metronomic; Administration, Oral; Antineoplastic Agents, Phytogenic; Biological Availability; Calorimetry, Differential Scanning; Drug Stability; Drug Storage; Excipients; Female; Half-Life; Humans; Male; Middle Aged; Neoplasms; Paclitaxel; Permeability; Povidone; Sodium Dodecyl Sulfate; Solubility; Spectroscopy, Fourier Transform Infrared; X-Ray Diffraction

Accurate identification of both abundant and rare proteins hinges on the development of single-protein sensing methods. Given the immense variation in protein expression levels in a cell, separation of proteins by weight would improve protein classification strategies. Upstream separation facilitates sample binning into smaller groups while also preventing sensor overflow, as may be caused by highly abundant proteins in cell lysates or clinical samples. Here, we scale a bulk analysis method for protein separation, sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE), to the single-molecule level using single-photon sensitive widefield imaging. Single-molecule sensing of the electrokinetically moving proteins is achieved by in situ polymerization of the PAGE in a low-profile fluidic channel having a depth of only ~ 0.6 µm. The polyacrylamide gel restricts the Brownian kinetics of the proteins, while the low-profile channel ensures that they remain in focus during imaging, allowing video-rate monitoring of single-protein migration. Calibration of the device involves separating a set of Atto647N-covalently labeled recombinant proteins in the size range of 14-70 kDa, yielding an exponential dependence of the proteins' molecular weights on the measured mobilities, as expected. Subsequently, we demonstrate the ability of our fluidic device to separate and image thousands of proteins directly extracted from a human cancer cell line. Using single-particle image analysis methods, we created detailed profiles of the separation kinetics of lysine and cysteine -labeled proteins. Downstream coupling of the device to single-protein identification sensors may provide superior protein classification and improve our ability to analyze complex biological and medical protein samples.

Topics: Acrylic Resins; Calibration; Cell Line, Tumor; Cysteine; Electrophoresis, Polyacrylamide Gel; Humans; Lysine; Molecular Weight; Neoplasms; Protein Array Analysis; Proteins; Proteomics; Sodium Dodecyl Sulfate

To achieve enhanced cancer therapy, a sequentially dynamic polymeric drug delivery system (ortho ester-linked PEGylated poly(disulfide)s-based micelle-doxorubicin (PS-g-OEMPEG-DOX)) is successfully constructed. The PEGylated micelle can keep stable in sodium dodecyl sulfate (SDS) solution at pH 7.4, but be prone to DePEGylation and dynamic size changes via the hydrolysis of ortho ester linkages in side chains at tumoral extracellular pH value (6.5). Moreover, the micelle can rapidly release DOX via the cleavage of poly(disulfide)s in backbone at intracellular reductive milieu (10 mmol/L of dithiothreitol (DTT)). The dynamic micelle with detachable PEGylation achieves the stable blood circulation, improved cellular uptake and cytotoxicity, stronger in vitro penetration and inhibition of tumoral multicellular spheroids, and significant in vivo tumor accumulation and inhibition while decreasing side effects. Thus, the sequentially dynamic polymeric micelle with detachable PEGylation can be considered as a promising and effective drug delivery system in cancer therapy.

Topics: Animals; Antineoplastic Agents; Cell Line, Tumor; Dithiothreitol; Doxorubicin; Drug Carriers; Drug Delivery Systems; Hep G2 Cells; Humans; Hydrogen-Ion Concentration; Hydrolysis; Male; Mice; Mice, Inbred ICR; Micelles; Neoplasms; Polyethylene Glycols; Polymers; Sodium Dodecyl Sulfate

Inhibitors against multidrug resistance (MDR) efflux transporters have failed in most clinical settings due to unfavorable pharmacokinetic interactions with co-administered anti-cancer drug and their inherent toxicities. Nanoparticles (NPs) have shown potential to overcome drug efflux by delivering and localizing therapeutic molecules within tumor mass. In this work, we investigated effect of nanocarrier surface charge and formulation parameters for a hydrophilic and lipophilic MDR inhibitor on their ability to reverse drug resistance. Active inhibition of efflux pumps was achieved by encapsulating first and third generation P-gp inhibitors- verapamil and elacridar respectively in non-ionic, anionic and cationic surfactant-based NPs. The ability of NPs to reverse P-glycoprotein (P-gp)-mediated MDR efflux was evaluated in sensitive (A2780) and resistant (A2780Adr) ovarian cancer cell lines by various in vitro accumulation and cytotoxicity assays. Uptake mechanism for NP appears to be caveolae-dependent with 20%-higher internalization in A2780Adr than A2780 cell lines which can be co-related to the biophysical membrane composition. Cationic- CTAB NPs showed highest reversal efficacy followed by PVA and SDS-NP (P+S NP) and PVA-NPs. As compared to doxorubicin treated drug resistant cells lines, blank-, verapamil- and elacridar-CTAB-NPs showed 2.6-, 20- and 193-fold lower IC50 values. This work highlights the importance of inhibitor-loaded charged particles to overcome cancer drug resistance.

Topics: Acridines; Antibiotics, Antineoplastic; ATP Binding Cassette Transporter, Subfamily B, Member 1; Cell Line, Tumor; Cell Survival; Doxorubicin; Drug Carriers; Drug Resistance, Neoplasm; Humans; Nanoparticles; Neoplasms; Polyvinyl Alcohol; Sodium Dodecyl Sulfate; Surface-Active Agents; Tetrahydroisoquinolines; Verapamil

A procedure based on micellar liquid chromatography has been developed to monitor five tyrosine kinase inhibitors in plasma, prescribed against several kinds of cancer: erlotinib, imatinib, sunitinib, sorafenib and lapatinib. The sample was diluted in a micellar solution and directly injected, thus clean-up steps were not required. The analytes were resolved without interferences in <20 min using a C18 column and a mobile phase of 0.13 M SDS-4% 1-butanol, buffered at pH 3.5, running under isocratic mode at 1 mL/min. The detection was performed by UV-visible absorbance, using a wavelength program to maximize the signal-to-noise ratio. The method was validated following the guideline of the European Medicines Agency in terms of: selectivity, calibration range (0.05-5 μg/mol), linearity (r(2)>0.990), limit of detection (15-35 ng/mL), carry-over effect, accuracy (-10.4 to +11.0%), precision (<9.2%), matrix effect, robustness (<8.4%) and stability. The procedure is rapid, easy-to-handle, uses a low amount of toxic chemical provide reliable results. Finally, the method was successfully used to analyze the studied tyrosine kinase inhibitors in plasma from cancer patients.

Topics: Antineoplastic Agents; Blood Chemical Analysis; Butanols; Calibration; Chromatography, Liquid; Europe; Humans; Hydrogen-Ion Concentration; Limit of Detection; Micelles; Neoplasms; Practice Guidelines as Topic; Protein Kinase Inhibitors; Protein-Tyrosine Kinases; Societies, Medical; Sodium Dodecyl Sulfate

In this study, the effects of the size and Chinese traditional processing (including elutriation, water cleaning, acid cleaning, alkali cleaning) on realgar nanoparticles (RN)-induced antitumor activity in human osteosarcoma cell lines (MG-63) and hepatoma carcinoma cell lines (HepG-2) were investigated. The human normal liver cell line (L-02) was used as control. RN was prepared by high-energy ball milling technology. The results showed that with the assistance of sodium dodecyl sulfate, the size of realgar could be reduced to 127 nm after 12 hours' ball milling. The surface charge was decreased from 0.83 eV to -17.85 eV and the content of As₂O₃ clearly increased. Except for elutriation, the processing methods did not clearly change the size of the RN, but the content of As₂O₃ was reduced dramatically. In vitro MTT tests indicated that in the two cancer cell lines, RN cytotoxicity was more intense than that of the coarse realgar nanoparticles, and cytotoxicity was typically time- and concentration-dependent. Also, RN cytotoxicities in the HepG-2 and L-02 cells all increased with increasing milling time. Due to the reduction of the As₂O₃ content, water cleaning, acid cleaning, and alkali cleaning decreased RN cytotoxicity in HepG-2, but RN after elutriation, with the lowest As₂O₃ (3.5 mg/g) and the smallest size (109.3 nm), showed comparable cytotoxicity in HepG-2 to RN without treatment. Meanwhile, RN-induced cytotoxicity in L-02 cells was clearly reduced. Therefore, it can be concluded that RN may provide a strong antiproliferation effect in the MG-63 and HepG-2 cells. Elutriation processing is a suitable approach to limit the dangerous side-effects of As₂O₃, while maintaining the effectiveness of RN.

Topics: Apoptosis; Arsenicals; Cell Line, Tumor; Cell Survival; Dose-Response Relationship, Drug; Drug Compounding; Flow Cytometry; Humans; Hydrogen-Ion Concentration; Nanoparticles; Neoplasms; Particle Size; Sodium Dodecyl Sulfate; Spectroscopy, Fourier Transform Infrared; Sulfides; X-Ray Diffraction

A microchip fluorescence-enhanced immunoassay method was developed for simultaneous detection of carcinoma antigen 125 (CA125) and carbohydrate antigen 15-3 (CA15-3). In this method, CA125 and CA15-3 react with excess amount of fluorescein isothiocyanate (FITC)-labeled monoclonal antibodies (Ab(*)) of CA125 and CA15-3 to form CA125-Ab(125)(*) and CA15-3-Ab(15-3)(*) complexes. Microchip electrophoresis (MCE) separation of free Ab(125)(*), Ab(15-3)(*), and CA125-Ab(125)(*), CA15-3-Ab(15-3)(*) complexes were then performed. The separated species were sensitively detected by laser-induced fluorescence detection (LIF). CA125 and CA15-3 were quantified simultaneously by measuring the fluorescence intensity of CA125-Ab(125)(*) and CA15-3-Ab(15-3)(*) complexes, respectively. Under the optimum conditions, the limits of detection were 0.23 U/mL for CA125 and 0.09 U/mL for CA15-3. The present MCE-LIF method was applied to the determination of CA125 and CA15-3 in serum from healthy subjects and cancer patients. The levels of CA125 and CA15-3 in these sera samples were found to be in the ranges of 15.6-36.1 U/mL and 13.8-28.4 U/mL for healthy subjects, and 192.5-368.3 U/mL and 63.3-198.4 U/mL for cancer patients.

Topics: Antibodies, Monoclonal; Antigen-Antibody Complex; Biomarkers, Tumor; CA-125 Antigen; Electrophoresis, Microchip; Fluorescein-5-isothiocyanate; Humans; Immunoassay; Mucin-1; Neoplasms; Reproducibility of Results; Sensitivity and Specificity; Sodium Dodecyl Sulfate; Spectrometry, Fluorescence

Carcinoembryonic antigen (CEA) as one of the most widely used tumor markers is used in the clinical diagnosis of colorectal, pancreatic, gastric, and cervical carcinomas. We describe a microchip electrophoresis (MCE)-based noncompetitive immunoassay technique for assaying CEA in human serum for cancer diagnosis.. Based on a noncompetitive immunoassay format, CEA reacts first with an excess amount of monoclonal antibody (Ab(1)), then free Ab(1) and the bound CEA-Ab(1) complex react with an excess amount of fluorescein isothiocyanate (FITC)-labeled secondary antibody (Ab(2)*) to form CEA-Ab(1)-Ab(2)* and Ab(1)-Ab(2)* complexes. Finally, the free Ab(2)* and bound CEA-Ab(1)-Ab(2)*, Ab(1)-Ab(2)* complexes were separated and detected by MCE coupling laser-induced fluorescence (LIF), and CEA was quantified by measuring the fluorescence intensity of CEA-Ab(1)-Ab(2)*.. The linear range for CEA was 60pg/ml-8ng/ml with a correlation coefficient of 0.9992 and a detection limit of 45.7pg/ml. The immunocomplex including CEA-Ab(1)-Ab(2)*, Ab(1)-Ab(2)*and free Ab(2)* was separated within 80s. The amounts of CEA in normal person serum were found to be in the range of 2.9-5.1microg/l, and seven cancer patients serum were analyzed, and CEA levels range from 79.6-270.1ng/ml.. This method may become a useful tool for rapid analysis of CEA and other tumor markers in biomedical analysis and clinical diagnosis.

Topics: Antibodies, Monoclonal; Blood Chemical Analysis; Buffers; Carcinoembryonic Antigen; Electricity; Electrophoresis; Fluorescein-5-isothiocyanate; Humans; Hydrogen-Ion Concentration; Immunoassay; Injections; Microchip Analytical Procedures; Neoplasms; Sodium Dodecyl Sulfate; Spectrometry, Fluorescence; Time Factors

A method for producing high-molecular-weight DNA from pulverized tissue, nuclear fractions, or cultured cells. This isolation method relies on the powerful proteolytic activity of proteinase K combined with the denaturing ability of the ionic detergent sodium dodecyl sulfate. Ethylenediaminetetraacetic acid is included in the lysis buffer to inhibit DNases.

Topics: DNA, Neoplasm; Endopeptidase K; Humans; Neoplasms; Sodium Dodecyl Sulfate; Surface-Active Agents

Topics: Automation; Biomarkers, Tumor; Chromatography, Affinity; Chromatography, High Pressure Liquid; Creatinine; Electrophoresis, Capillary; Female; Humans; Indicators and Reagents; Male; Neoplasms; Nucleosides; Reference Values; RNA; RNA, Neoplasm; Sodium Dodecyl Sulfate

This paper gives a capillary electrophoretic method for the separation of 15 urinary normal and modified nucleosides from cancer patients in less than 40 min. A 500 mm x 50 microns uncoated capillary column (437.5 mm to window) was used. The effects of the voltage and the sodium dodecyl sulfate (SDS) concentration in the buffer on the separation were studied. With reproducibilities of migration times better than 1.2% (R.S.D.) and determined concentrations better than 5-25%, depending on the concentrations of nucleosides in the urine, the analytical characteristics of the method were good. Using this developed method, the concentrations of 13 normal and modified nucleosides, extracted on a phenyl boronic acid affinity chromatography column, in 25 urines from patients of 14 kinds of cancer were determined. The levels (nmol/mumol creatinine) of modified nucleosides in urines from cancer patients were increased as compared with those in normal urines.

Topics: Chromatography, Affinity; Electrophoresis, Capillary; Female; Humans; Male; Neoplasms; Nucleosides; Reproducibility of Results; Sodium Dodecyl Sulfate

Matrix metalloproteinases (MMPs) have been implicated in mechanisms of metastasis in experimental cancer models and in human malignancies. In this study, we used substrate gel electrophoresis (zymography) to determine the frequency of detection of MMPs in urine of patients with a variety of cancers. Three molecular weight classes of urinary MMPs, Mr 72,000, Mr 92,000, and high molecular weight (Mr > or = 150,000) species, were detected reproducibly and correlated with disease status. The Mr 72,000 and Mr 92,000 species were identified as MMP-2 and MMP-9, respectively, by Western blot analysis. The presence of biologically active MMP-2 (P < 0.001) or MMP-9 (P = 0.002) was an independent predictor of organ-confined cancer, and the high molecular weight species (P < 0.001) was an independent predictor of metastatic cancer. This is the first study to demonstrate that analysis of urinary MMPs may be useful in determining disease status in a variety of human cancers, both within and outside of the urinary tract.

Topics: Adult; Aged; Aged, 80 and over; Breast Neoplasms; Collagenases; Electrophoresis, Polyacrylamide Gel; Female; Gelatinases; Humans; Kidney Neoplasms; Male; Matrix Metalloproteinase 2; Matrix Metalloproteinase 9; Metalloendopeptidases; Middle Aged; Neoplasm Proteins; Neoplasms; Prostatic Neoplasms; Sensitivity and Specificity; Sodium Dodecyl Sulfate; Substrate Specificity; Urinary Bladder Neoplasms

We describe the construction of a recombinant bispecific antibody fragment in the diabody format with specificity for both the well-established human pancarcinoma associated target antigen EGP2 (epithelial glycoprotein 2, also known as the CO17-1A antigen or KSA) and the CD3epsilon chain of human TCR/CD3 complex. The murine anti-EGP2 (MOC31) single chain variable fragment (scFv) and the humanized anti-CD3 (Ucht1v9) scFv were cast into a diabody format (designated Dia5v9) using a short 5 amino acid Gly-Ser linker between immunoglobulin heavy-chain and light-chain variable domains. Purification of the poly-histidine tagged Dia5v9 was achieved from extracts of protease deficient Escherichia coli by IMAC chromatography. The Dia5v9 diabody showed strong binding to both EGP2 and CD3 in transfected cells. The in vitro efficacy of Dia5v9 in mediating tumor cell lysis by interleukin-2 activated human T cells appeared to be similar to that of the hybrid-hybridoma-derived BsF(ab')2 Bis1 (anti-EGP2/anti-CD3) in a standard 4-hr 51Cr-release assay. This small and partially humanized recombinant bispecific antibody fragment may be valuable for T-cell-based immunotherapeutical treatment protocols, retargeting activated peripheral blood T lymphocytes to lyse various human carcinomas in vivo.

Topics: Animals; Antibodies, Bispecific; Antibody Specificity; Antigens, Neoplasm; Chromatography, Gel; COS Cells; Electrophoresis, Polyacrylamide Gel; Humans; Immunization, Passive; Immunoglobulin Fragments; Lymphocyte Activation; Neoplasms; Recombinant Proteins; Sodium Dodecyl Sulfate; T-Lymphocytes; T-Lymphocytes, Cytotoxic

The oncogenic protein Bcl-2 functions as a potent inhibitor of programmed cell death. This survival activity has been shown in some settings to be influenced by the Bcl-2 phosphorylation state. It has been demonstrated that treatment with microtubule-targeted agents results in phosphorylation of both Raf-1 kinase and Bcl-2. The Bcl-2-related family member Bcl-xL also exhibits a death suppressive activity, but its potential for phosphorylation following exposure to drugs that interact with microtubules has not been evaluated. Several tumor cell lines with low or undetectable levels of Bcl-2 protein expression were found to express Bcl-xL. A more slowly migrating Bcl-xL band was observed on immunoblots after cells were treated with microtubule-targeted agents. The appearance of this band was responsive to dose and was absent when the cell lysates were treated with lambda protein phosphatase. Using a Bcl-xL-specific monoclonal antibody, the phosphorylated form of Bcl-xL was immunoprecipitated from cells treated with paclitaxel and metabolically labeled with 32P-labeled inorganic orthophosphate. Herein, we report that Bcl-xL is phosphorylated in malignant cells after incubation with agents that target tubulin, including paclitaxel, vincristine, vinblastine, colchicine, and nocodazole. Moreover, paclitaxel-resistant ovarian carcinoma cell lines that have mutations in tubulin failed to exhibit phosphorylation of Bcl-xL after paclitaxel exposure, but they did demonstrate Bcl-xL phosphorylation in the presence of other tubulin-targeting agents. As observed for Bcl-2, phosphorylation of Bcl-xL was accompanied by phosphorylation of Raf-1. Interestingly, phosphorylation of these three proteins failed to occur or was much less pronounced when cells grown at high density were challenged with drug. Also, reduced Raf-1 expression, observed after treatment of cells with geldanamycin prior to and during incubation with the microtubule-active drugs, correlated with diminished Bcl-xL phosphorylation. Taken together, these results suggest that Bcl-xL, like Bcl-2, is phosphorylated by agents that disrupt microtubule architecture. By analogy with Bcl-2, this phosphorylation may play a critical role in modulating Bcl-xL function and may be an important determinant of microtubule-directed chemotherapeutic efficacy in human tumors.

Topics: Antibiotics, Antineoplastic; Antineoplastic Agents, Phytogenic; bcl-X Protein; Benzoquinones; Cell Count; Drug Resistance, Neoplasm; Electrophoresis, Polyacrylamide Gel; Humans; Lactams, Macrocyclic; Microtubules; Neoplasm Proteins; Neoplasms; Paclitaxel; Phosphoprotein Phosphatases; Phosphorus Radioisotopes; Phosphorylation; Protein Processing, Post-Translational; Proto-Oncogene Proteins c-bcl-2; Proto-Oncogene Proteins c-raf; Quinones; Sodium Dodecyl Sulfate; Tubulin; Tumor Cells, Cultured

Topics: Consumer Product Safety; Cosmetics; Hair Preparations; Humans; Neoplasms; Sodium Dodecyl Sulfate; United States; United States Food and Drug Administration

Volumetric titration of aqueous solutions of haematoporphyrin IX (HP) yields two inflexion points, whereas four pK values can be obtained via mathematical fitting of the experimental data. Assignment of all pK protonation sites is made. A zwitterion is proposed as the neutral species of HP. Evaluation of the pK values of HP in the presence of sodium dodecyl sulphate (SDS) leads to a drastically altered ionic species distribution. On the basis of the distribution diagrams obtained, a pH-sensitive twofold mechanism is proposed for the selective biodistribution of porphyrin-type photochemotherapeutic agents, one involving tissue distribution and the other involving cell membrane penetration by the neutral zwitterion.

Topics: Acid-Base Equilibrium; Cell Membrane; Hematoporphyrins; Hydrogen-Ion Concentration; Models, Chemical; Neoplasms; Sodium Dodecyl Sulfate; Tissue Distribution

Tissue polypeptide antigen (TPA) is a complex protein which has been originally identified in extracts of pooled tumors using horse antisera raised against the insolubles of human tumor cells. The antigen is now routinely detected and measured by a previously described hemagglutination inhibition assay. It has been shown by this method that the concentration of the antigen is higher in tumor tissues and in sera of cancer patients as compared to normal tissues or normal sera, respectively. In aqueous solutions, pH 2-12, TPA has a tendency to form high molecular weight aggregates. However they can be dissociated in sodium dodecyl sulfate into subunits, each appearing as a single chain peptide: B1 (Mr 4.3 x 10(4)), B2 (Mr 3.0 x 10(4)), C (Mr 1.7 x 10(4)). The subunits saturate anti-TPA serum indistinguishably from TPA. Amino acid composition of TPA and subunits is dominated by glutamic acid, aspartic acid and leucine, cysteine being absent in subunit B1. The isoelectric point of the main subunit, B1, is 4.4-4.6. Sedimentation and diffusion analyses indicate that pure subunit B1 in aqueous solution exists in distinct oligomeric states.

Topics: Amino Acids; Chromatography, Ion Exchange; Electrophoresis, Polyacrylamide Gel; Humans; Isoelectric Focusing; Molecular Weight; Neoplasms; Peptides; Sodium Dodecyl Sulfate; Tissue Distribution; Tissue Polypeptide Antigen

The interaction of the highly purified basic protein "antigen", calf thymus histone F2A1 fraction, with peripheral lymphocytes isolated from patients with cancer and from normal subjects has been studied. Analysis, by SDS polyacrylamide gel electrophoresis of the basic protein remaining in the supernatant fluid after interaction with low concentrations of lymphocytes from patients showed the presence of a component(s) of molecular weight smaller than the original histone F2A1 fraction. Similar experiments using lymphocytes derived from normal subjects indicated that this component(s) is absent, or at least is present in only small amounts. This difference could be partially abolished by using high concentrations of cell preparations. It is suggested that the observed difference is due at least in part, to differences in protease activity between the two preparations. The possible significance of these findings in relation to the macrophage electrophoretic mobility test for cancer is discussed.

Topics: Animals; Antigens; Cattle; Electrophoresis, Polyacrylamide Gel; Histones; Humans; Iodine Radioisotopes; Lymphocytes; Molecular Weight; Neoplasms; Peptide Fragments; Proteins; Sodium Dodecyl Sulfate; Thymus Gland

Topics: Adolescent; Adult; Aged; Benzalkonium Compounds; Breast Neoplasms; Croton Oil; Dermatitis, Contact; Female; Humans; Lung Neoplasms; Male; Middle Aged; Neoplasm Metastasis; Neoplasms; Skin Tests; Sodium Dodecyl Sulfate

Topics: Detergents; HeLa Cells; Humans; Neoplasms; Poliomyelitis; Poliovirus; Sodium Dodecyl Sulfate