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Biomedical subjects

M Macklin

Publications and source records attributed to M Macklin.

At least 19 recordsLinked to original sources
PubMed2001

Characterisation of single domain ATP-binding cassette protien homologues of Theileria parva.

Two distinct genes encoding single domain, ATP-binding cassette transport protein homologues of Theileria parva were cloned and sequenced. Neither of the genes is tandemly duplicated. One gene, TpABC1, encodes a predicted protein of 593 amino acids with an N-terminal hydrophobic domain containing six potential membrane-spanning segments. A single discontinuous ATP-binding element was located in the C-terminal region of TpABC1. The second gene, TpABC2, also contains a single C-terminal ATP-binding motif. Copies of TpABC2 were present at four loci in the T. parva genome on three different chromosomes. TpABC1 exhibited allelic polymorphism between stocks of the parasite. Comparison of cDNA and genomic sequences revealed that TpABC1 contained seven short introns, between 29 and 84 bp in length. The full-length TpABC1 protein was expressed in insect cells using the baculovirus system. Application of antibodies raised against the recombinant antigen to western blots of T. parva piroplasm lysates detected an 85 kDa protein in this life-cycle stage.

ATP Binding Cassette Transporter 1↗
PubMed1998

Cloning and characterization of a 150 kDa microsphere antigen of Theileria parva that is immunologically cross-reactive with the polymorphic immunodominant molecule (PIM).

To identify the genes encoding novel immunodominant antigens of Theileria parva a lambda gt11 library of piroplasm genomic DNA was immunoscreened with bovine recovery serum and a gene encoding a 150 kDa antigen (p150) was identified. The predicted polypeptide contains an N-terminal secretory signal sequence and a proline-rich region of repeated amino acid motifs. The repeat region is polymorphic between stocks of T. parva in both copy number and sequence, and analysis of the repeat region from 10 stocks of T. parva revealed 5 p150 variants. A monoclonal antibody (mAb) against the T. parva polymorphic immunodominant molecule (PIM) cross-reacted with the recombinant p150. The p150 has sequence homology with a PIM peptide sequence containing the anti-PIM mAb epitope. Immunoelectron microscopy demonstrated that the p150 antigen, like PIM, is located in the microspheres of the sporozoites and is exocytosed following sporozoite invasion of the host lymphocyte. By immunoelectron microscopy p150 was subsequently transiently detectable on the sporozoite surface and in the lymphocyte cytosol. Immunoblotting showed that p150 is also expressed by the schizont stage, but at much lower levels compared to the sporozoite. These results suggest a major role for p150 in the early events of host-sporozoite interaction.

Amino Acid Sequence↗
PubMed1987

Cocaine.

This article discusses cocaine as America's leading illicit drug of abuse. Cocaine pharmacology, metabolism, and methods of administration are related to medical symptoms and complications of use. Reasons for increased use as well as signs suggestive of individual abuse are given, and treatment issues specific to cocaine are discussed. Urine testing for cocaine and other abused drugs is encouraged, and specific reliable techniques are suggested.

Adolescent↗
PubMed1984

Structural homology between Drosophila melanogaster and Escherichia coli acidic ribosomal proteins.

Antibodies raised against Drosophila melanogaster ribosomal proteins (r-proteins) were used to examine possible structural relationships between eukaryotic and prokaryotic r-proteins. The antisera were raised against either groups of r-proteins or individually purified r-proteins. Two antisera showed a cross-reaction with total Escherichia coli r-proteins in Ouchterlony double immunodiffusion assays: an antiserum against the D. melanogaster small subunit protein S14 (anti-S14) and an antiserum against a group of D. melanogaster r-proteins (anti-TP80). The specificity of the antisera and the identity of the homologous E. coli r-proteins were characterized by using immunooverlay and immunoblot assays. These assays indicated that anti-S14 was highly specific for protein S14 and anti-TP80 was a multispecific serum that recognized several of the D. melanogaster ribosomal proteins. The E. coli protein homologous to D. melanogaster protein S14 was identified as E. coli protein S6. By adsorption of the anti-TP80 serum, we determined that D. melanogaster protein 7/8 is homologous to the acidic E. coli protein L7/L12. D. melanogaster acidic protein 13 was also shown to be immunologically related to D. melanogaster protein 7/8.

Animals↗
PubMed1980

Group fractionation and determination of the number of ribosomal subunit proteins from Drosophila melanogaster embryos.

Proteins were extracted from ribosomes and (for the first time) from ribosomal subunits of Drosophila melanogaster embryos. The ribosomal proteins were analyzed by two-dimensional polyacrylamide gel electrophoresis. The electrophoretograms displayed 78 spots for the 80S monomers, 35 spots for the 60S subunits, and 31 spots for the 40S subunits. On the basis of present information, we propose what we believe to be a reliable and convenient nomenclature for the proteins of the ribosomes and each of the subunits. A pair of acidic proteins from D. melanogaster appears to be very similar in electrophoretic mobility to the acidic proteins L7/L12 from Escherichia coli and L40/L41 from rat liver. The electrophoretogram of proteins from embryonic ribosomes shows both qualitative and quantitative differences from those of larvae, pupae, and adults previously reported by others. The proteins of the 40S subunit range in molecular weight from approximately 10,000 to 50,000, and those from the 60S subunit range from approximately 11,000 to 50,000.

Animals↗
PubMed1977

Changes in the conduction of the fetal electrocardiogram to the maternal abdominal surface during gestation.

A technique for recording high-quality vectorcardiograms from the fetus in utero is described. A study was conducted to clarify conflicting views on the mechanism of fetal electrocardiogram (FECG) signal transmission to the maternal abdominal surface during the latter half of gestation. The results of this study support the view that a general pattern of uniform conduction of FECG currents exists between 20 and 28 weeks' gestation in most subjects, that signal magnitudes decrease markedly between 28 and 34 weeks' gestation and conduction tends to behave as if it is nonuniform through the maternal abdominal volume, and that a preferred signal pathway, possibly through the oronasal cavities of the fetus, appears to develop after 34 weeks' gestation and continues until term. Two different abdominal FECG lead systems are recommended on the basis of these findings which should maximize the accuracy of FECG monitoring of the preterm fetus.

Abdomen↗
PubMed1973

Water excretion by hydra.

Hydra were cut so that regenerates consisting only of the central gastric region were formed. This region, which has no natural opening to the environment, is capable of osmoregulation and of removing excess fluid from the gut. The fluid is excreted through a break in the body wall created as a result of a strong contraction when the gut is distended with fluid. A normal hydra, therefore, must remove excess fluid by contracting and expelling it through its mouth.

Animals↗