The homogenous γG-immunoglobulin produced by mouse plasmacytoma 5563 and its subsequent heterogeneity in serum

The mouse plasma cell tumour 5563 has been shown to synthesize and secrete a single molecular species of gammaG-immunoglobulin, which was identified by labelling with (14)C-labelled amino acids. The heterogeneity of G-myeloma globulin as it is found in serum of tumour-bearing mice is due to subsequent changes in the charge properties of the newly secreted molecules. These changes have been reproduced in vitro. On incubation with sterile serum, the newly formed radioactive myeloma protein changed its chromatographic and electrophoretic properties to coincide with those of myeloma protein isolated from serum. Incubation of purified myeloma protein band a, under a variety of conditions, led to the characteristic pattern of serum myeloma protein showing multiple electrophoretic bands. The chemical nature of the molecular changes is not yet known. It is suggested that seruminduced changes could contribute to the electrophoretic heterogeneity of specific antibodies within the gammaG-class of immunoglobulins. This demonstration of the production of a single molecular species of immunoglobulin by a plasma cell tumour provides support for the concept of ;one-cell-one antibody'.     

The Latex Serologic Test for Syphilis—A New Screening Procedure

A new macroscopic screening test for syphilis, the Latex-sts test, is extraordinarily simple. After inactivation of the patient''s serum for 30 minutes at 56°C the test is performed by mixing the patient''s serum with latex particles coated with cardiolipin and a protein fraction obtained from the non-pathogenic Reiter strain of Treponema pallidum. Two to three minutes after mixing, the result of the test is observed on a ringed serologic plate. The sensitivity, specificity and reproducibility of the new test are equivalent to those of the qualitative Venereal Disease Research Laboratory tube test. The advantages of the Latex-sts are that it can be done in a short time, it is simple and it requires a minimum of laboratory equipment. The coated latex particles are stable for 12 months.     

Effect of lowered incubation temperatures on nucleic acid and protein synthesis by a mesophilic and a psychrophilic bacterium

The authors studied changes in the synthesis of nucleic acids (RNA, DNA) and protein by a mesophilic strain ofEscherichia coli B and a psychrophilic strain ofPseudomonas fluorescens at a low incubation temperature giving tenfold prolongation of the generation time. It was found that lowering the incubation temperature was followed by an increase in the intracellular nucleic acid content during the lag phase and the phase of accelerated growth, in which maximum nucleic acid (NA) values were reached. As a result, the total NA level in the cell also remained relatively high during further proliferation, when the increase in NA (particularly RNA) slows down at low incubation temperatures. Proteosynthesis, however, fell in the mesophilic culture. The smaller effect of a lowered temperature on DNA biosynthesis was manifested specifically in the lag phase ofEscherichia coli, in which disproportion developed between the amount of DNA (which was synthesized at a relatively higher rate) and RNA; this was afterwards equalized by a temporary break in DNA production. Pronounced differences in the given types of biosynthesis were found only in the mesophilic culture, while at suboptimal temperatures the metabolism of the psychrophilic strain slowed down but no marked changes occurred.     

Zum Abbau der l-Äpfelsäure durch Milchsäurebakterien

Zusammenfassung Die Abtrennung der OES-Decarboxylase vom Malic-Enzym wird bei Enzymlösung aus Bakterien des Stammes Lactobacillus plantarum L durchgeführt. Die Trennung gelingt wegen der unterschiedlichen Temperatur-und pH-Empfindlichkeit der beiden Enzyme. Das Malic-Enzym ist im Bereich von pH 4,5–5,0 nur dann bei 40° C und darüber vor Denaturierung geschützt, wenn es als Substrat-NAD⁺-Mn⁺⁺-Komplex vorliegt. Die OES-Decarboxylase ist entsprechend temperaturstabiler als das Malic-Enzym, auch wenn keine Oxalessigsäure zugesetzt wird.Die Ammoniumsulfat-Fraktionierung bringt keine befriedigende Trennung der Enzyme mit sich. Wird das Malic-Enzym durch Denaturierung nicht entfernt, so reißt es bei 75% iger Sättigung mit Ammoniumsulfat die OES-Decarboxylase mit in den Niederschlag. Bei dieser Salzkonzentration fällt auch die Malat-Dehydrogenase aus.Mikrobiolosisch und papierchromatographisch durchgeführte Biotinnachweise bestätigen, daß die OES-Decarboxylase des Stammes, L ein Biotinproteid ist.