Clinical comparison of radiolocalization of two monoclonal antibodies (mAbs) against the TAG-72 antigen

Ten patients with colorectal cancer metastases received 125I-B72.3 and 131I-CC49 prior to laparotomy (five patients received 1 mg, and five 20 mg of each mAb). Tumor:serum ratios of 131I-CC49 were better than those of 125I-B72.3 (P < 0.01 at 1 mg; P = 0.05 at 20 mg; P < 0.01 at both doses). All known lesions > or = 1 cm in diameter were visualized at the 20 mg dose. There was no difference in absolute tumor uptake of 125I-B72.3 or 131I-CC49. We conclude that mAb CC49 has better relative uptake in colorectal cancers than mAb B72.3.     

An electron-microscopic study of Herpetomonase sp. (Leptomonas pessoai)

The fine structure of the promastigotes of Herpetomonas sp. (Leptomonas pessoai) kept in a defined medium at 28 degrees C is described. This portozoon reveals several features in common with other trypanosomatids. A membrane-bounded organelle measuring 0.2 to 0.8 mum in diameter, similar to that described as peroxisome in Crithidia fasciculata, was also observed. A large cavity, located between the nucleus and the kinetoplast and containing vesicles and small particulate material is discussed in this paper.     

Magnetic properties of iron alloys

The purpose of this work was to compare the properties of high purity atomized iron powder compacts with conventional high purity irons and to show the effects of porosity on magnetic properties. It was found that if powders were hot repressed so that no porosity was present, the magnetic properties were as good as or better than conventional high purity irons, depending on the sintering conditions employed. Intrinsic properties were similar because the amount of iron available to magnetize was equivalent. Structure-sensitive properties depended on the grain size. If the compacts were sintered above the delta transition temperature, these properties were equivalent to the purest of the conventional high purity irons. As the compacts became less dense and more porosity was present, induction and remanent magnetization decreased linearly with density; resistivity increased. In the case of structure-sensitive properties, porosity restricted grain growth. Small, closely spaced pores caused the greatest degradation of properties. Equations were derived through regression analyses and were found to explain more than 90% of the data. The intrinsic properties: induction, remanent magnetization, and resistivity were all linear functions of the density. The maximum permeability and the coercive force were power functions of the mean grain size intercept. These equations provide a basis for design of magnetic components using P/M compacts. If the properties that are desired are known, the density or the grain size required may be calculated. From this, the powder and the processing conditions required can be established to provide the desired properties.     

Interaction of non-histone chromosomal proteins HMG1 and HMG2 with DNA

Interaction between non-histone protein HMG1 or HMG2 and DNA has been studied by using thermal denaturation and circular dichroism (CD) spectroscopy. We have made the following observations. 1. The binding of each of these two proteins to DNA stabilizes the latter, as shown by an increase in melting temperature of 20 degrees C (from 45 degrees C to about 65 degrees C). 2. There are 6.0 amino acids/nucleotide in HMG1-bound DNA and 5.0 in HMGI-bound DNA which suggests that each HMB1 moleculae would cover about 20 base pairs of DNA and each HMG2 molecule would cover about 25 base pairs. 3. The alpha-helical content of these two non-histone proteins in the complexes, estimated from the CD value at 220 nm, is about one third to one half that of total proteins in calf thymus chromatin. 4. DNA conformation is distorted only slightly by the binding of protein HMG1 or HMG2. 5. Neither the melting nor the CD properties of HMG1-DNA or HMG2-DNA complexes differ substantially whether they are prepared by NaCl-gradient dialysis in urea or by direct mixing of protein and DNA at 0.15 M NaCl, followed by dialysis against the same buffer i.e. 0.25 mM EDTA (pH 8.0).