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Biomedical subjects

M Kondo

Publications and source records attributed to M Kondo.

At least 1,495 records · Page 83Linked to original sources
PubMed1975

Streptococcal preparation as an activator of host-mediated immune response: cellular immunity and alternate pathway of complement.

Streptococcal preparation, OK-432, was examined for its ability to initiate a host-mediated immune response. Aged individuals with negative skin response to phytohemagglutinin (PHA), as well as reduced in vitro blastoid transformation of lymphocytes, were treated with OK-432, and the response to PHA appeared in two out of three cases. The preparation was also demonstrated to convert C3 proactivator of complement when incubated with fresh human serum, as tested by immunoelectrophoresis, indicating the possibility that OK-432 might activate the alternate pathway of complement.

Aged↗
PubMed1975

Structure and function of RNA replicase of bacteriophage Qbeta.

(1) The RNA replicase induced by bacteriophage Qbeta consists of four non-identical subunits designated as alpha (mol. wt. 74000), beta (mol. wt. 64000), gamma (mol. wt. 47000) and delta (mol. wt. 33000), only one (subunit beta) of which is specified by the phage genome. (2) Subunit alpha (30 S ribosomal protein "S1" as well as translational interference factor "i") is required only for (+) strand-directed RNA synthesis in the presence of the host factor. (3) Qbeta replicase lacking subunit alpha (R-alpha) is capable of replicating templates other than (+) strand, such as (--), "6S" RNA, poly(C) etc., in the absence of the host factor. (4) Subunit beta is suggested to be the nucleotide-polymerizing enzyme, but is unable to initiate RNA synthesis by itself. (5) Subunits gamma and delta are identical to the protein synthesis elongation factors, EF-Tu and EF-Ts, respectively, and are required only for initiation of RNA synthesis, but not for elongation. (6) A model of Qbeta replicase is presented in order to discuss observed template-enzyme interactions.

Base Sequence↗
PubMed1975

Occurrence of phosphorylserine in the spore coat of Bacillus subtilis NRRL B558.

Phosphorylserine was isolated from the spores of Bacillus subtilis NRRL B 558. This phosphorylated amino acid was only found in the spore coat protein and was not detectable in vegetative cells. The compound was characteristically synthesized at a late stage of sporulation and its turnover did not occur until the completion of mature spore formation. The protein which contains phosphorylserine was not solubilized from the spore coat by digestion with pronase or treatment with any detergents.

Bacillus subtilis↗