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M Richardson

Publications and source records attributed to M Richardson.

At least 415 records · Page 23Linked to original sources
PubMed1972

The amino acid sequence of cytochrome c from Helix aspersa Müller (garden snail).

The amino acid sequence of a snail cytochrome c has been determined. The molecule consists of a single polypeptide chain of 104 residues, and is homologous with other mitochondrial cytochromes c. Unlike the cytochromes c from vertebrates, there is no acetyl blocking group at the N-terminus. A change in an otherwise invariant position has been observed in position 87. Comparison with amino acid sequences of cytochromes c from other sources indicates that the point of divergence of the molluscs and the vertebrates in evolutionary time was 720 million years ago. Experimental details are given in a supplementary paper that has been deposited as Supplementary Publication SUP 50009 at the National Lending Library for Science and Technology, Boston Spa, Yorks. LS23 7BQ, U.K., from whom copies can be obtained on the terms indicated in Biochem. J. (1972), 126, 5.

Amino Acid Sequence↗
PubMed1972

Prenatal immunization by the oral route: stimulation of Brucella antibody in fetal lambs.

No simple means exists for immunizing infants and large animals in utero. The feasibility of stimulating immune response by the oral route was investigated by using the fetal lamb as experimental model and Brucella as prototype antigen. Antigenic stimulation was assessed by serum agglutinin levels. Primary and secondary responses were elicited in fetal lambs by Brucella antigen introduced into the amniotic fluid 10 to 50 days prenatally. One lamb born 75 days after primary exposure in utero mounted a secondary response to antigen at 2 days of age. The evidence of immunization by the oral route suggests that local intestinal immunity also might be acquired in fetal life by this route.

Administration, Oral↗
PubMed1971

The amino acid sequence of rape (Brassica Napus L) cytochrome c.

The amino acid sequence of rape (Brassica Napus L) cytochrome c was determined using 1 mumole of protein. Analysis of chymotryptic and tryptic peptides by the dansyl-Edman method showed that the molecule consisted of 111 residues and was homologous with other mitochondrial plant cytochromes c. The amino acid sequence was found to be identical with that previously reported for the cytochrome c from cauliflower (Brassica oleracea L).

Amino Acid Sequence↗
PubMed1971

The amino acid sequence of sesame (Sesamum indicum L.) and castor (Ricinus communis L.) cytochrome c.

The amino acid sequences of sesame (Sesamum indicum L.) and castor (Ricinus communis L.) cytochrome c were determined by using 1.5mumol of protein from each species. Both molecules consist of a single chain of 111 amino acid residues and are homologous with other mitochondrial cytochrome c molecules. Both have an N-acetylated ;tail' of eight amino acids and two in-N-trimethyl-lysine residues, as also reported for wheat germ (Delange, Glazer & Smith, 1969) and mung-bean cytochrome c (Thompson, Laycock, Ramshaw & Boulter, 1970). Two different preparations of castor cytochrome c differed by one residue. This was glutamic acid for glutamine in position 100. The results for sesame and castor cytochrome c led to a re-examination and subsequent correction to the N-terminal region of the mung-bean cytochrome c sequence, as given by Thompson et al. (1970).

Amino Acid Sequence↗
PubMed1971

The amino acid sequence of cytochrome c from Cucurbita maxima L. (pumpkin).

The amino acid sequence of pumpkin cytochrome c was determined on 2mumol of protein. Some evidence was found for the occurrence of two forms of cytochrome c, whose sequences differed in three positions. Pumpkin cytochrome c consists of 111 residues and is homologous with mitochondrial cytochromes c from other plants. Experimental details are given in a supplementary paper that has been deposited as Supplementary Publication SUP 50005 at the National Lending Library for Science and Technology, Boston Spa, Yorks. LS23 7BQ, U.K., from whom copies can be obtained on the terms indicated in Biochem. J. (1971), 121, 7.

Amino Acid Sequence↗
PubMed1971

The amino acid sequence of cytochrome c of Fagopyrum esculentum Moench (buckwheat) and Brassica oleracea L. (cauliflower).

The amino acid sequences of buckwheat and cauliflower cytochromes c were determined on 1(1/2)mumol and 1mumol of protein respectively. The molecules consist of 111 residues and are homologous with other plant mitochondrial cytochromes c. Experimental details are given in a supplementary paper that has been deposited as Supplementary Publication SUP 50005 at the National Lending Library for Science and Technology, Boston Spa, Yorks. LS23 7BQ, U.K., from whom copies can be obtained on the terms indicated in Biochem. J. (1971), 121, 7.

Amino Acid Sequence↗
PubMed1971

The amino acid sequence of cytochrome c from Abutilon theophrasti Medic. and Gossypium barbadense L. (cotton).

The amino acid sequences of Abutilon and Gossypium cytochromes c were determined on 1mumol of protein. The molecules consist of 111 residues and are homologous with other mitochondrial plant cytochromes c. Experimental details are given in a supplementary paper that has been deposited as Supplementary Publication SUP 50005 at the National Lending Library for Science and Technology, Boston Spa, Yorks. LS23 7BQ, U.K., from whom copies can be obtained on the terms indicated in Biochem. J. (1971), 121, 7.

Amino Acid Sequence↗
PubMed1970

Intracellular Pasteurella pseudotuberculosis: Multiplication in Cultured Spleen and Kidney Cells.

Pasteurella pseudotuberculosis multiplied within rabbit cells in primary culture. Spleen cells from rabbits were either dispersed mechanically, exposed to the organism immediately after cell preparation, and grown as a pellet or the cells were dispersed enzymatically and grown as a monolayer for 4 to 6 days before the bacteria were introduced. Intracellular multiplication proceeded at a logarithmic rate for 1 to 2 days, with a generation time of about 70 min in pelleted cells and 4 to 5 hr in monolayered cells. Under the conditions employed, the wild-type virulent strain and an avirulent mutant multiplied at similar rates. Atmosphere, constituents of the medium, and multiplicity of infection influenced intracellular proliferation. The organism also proliferated in kidney cells. Microscopic observation of stained cells indicated limited growth of the pathogen in spleen cells at 37 C. In kidney cells, the pasteurellae localized in compartments; frequently, a single compartment with masses of proliferating organisms almost filled the cytoplasm.

Journal Article↗