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M J Frenkel

Publications and source records attributed to M J Frenkel.

35 records · Page 2Linked to original sources
PubMed1991

Unexpected sequence diversity in the amino-terminal ends of the coat proteins of strains of sugarcane mosaic virus.

The sequence of the 3'-terminal 1343 nucleotides of the SC strain of the sugarcane mosaic virus (SCMV-SC) genome was compared with the 1376 nucleotides at the 3' terminus of maize dwarf mosaic virus B (MDMV-B). The SCMV-SC sequence includes an open reading frame which codes for the viral coat protein of 313 amino acids (nucleotides 157 to 1116), followed by a 3' non-coding region of 235 nucleotides and a poly(A) tail. The MDMV-B sequence codes for the capsid protein (nucleotides 157 to 1139) of 328 amino acids and has a 3' non-coding region of 236 nucleotides. The coat protein of SCMV-SC has 92% identity with that of MDMV-B except for the region between amino acid residues 27 and 70 of SCMV-SC. This region of SCMV-SC is smaller (44 residues) than the equivalent region in MDMV-B (59 residues) and has only 22% identity with the MDMV-B sequence. Possible mechanisms for the generation of this sequence diversity are discussed. Despite this diversity, the sequence identities of both the major part of the coat proteins and the 3' non-coding regions confirm the proposal, based on previously described serological data, that SCMV-SC and MDMV-B are strains of SCMV.

Amino Acid Sequence↗
PubMed1990

Characterization, cloning and host-protective activity of a 30-kilodalton glycoprotein secreted by the parasitic stages of Trichostrongylus colubriformis.

The helminth Trichostrongylus colubriformis is a parasitic nematode infecting the small intestine of sheep. We report the isolation and characterization of a 30-kDa glycoprotein capable of partially protecting guinea-pigs against the parasite. This glycoprotein is secreted by the L4 and adult parasitic stages of the worm. The sequence of three separate cDNA clones predicts the polypeptide to be about 15 kDa, with four N-linked carbohydrate chains and an internal disulphide bond. The clones also indicate the existence of sequence variability in this antigen. Limited sequence homology to a porcine intestinal peptide suggests an influence on host gut physiology.

Amino Acid Sequence↗
PubMed1989

Coat protein of potyviruses. 6. Amino acid sequences suggest watermelon mosaic virus 2 and soybean mosaic virus-N are strains of the same potyvirus.

The amino acid sequence of the coat protein of watermelon mosaic virus 2 (WMV 2) was determined by a combination of peptide and nucleic acid sequencing. The coat protein of WMV 2 contained 281 amino acid residues including a single cysteine at position 132 and a blocked amino terminus. Comparison with the coat protein sequences of 20 strains of ten distinct potyviruses showed sequence homologies ranging from 43% to 69% except for the N strain of soybean mosaic virus (SMV-N), where the sequence homology with WMV 2 was 83%. This degree of homology and the location of sequence differences between WMV 2 and SMV-N is much closer to that observed between strains of the same virus than that found between distinct potyviruses. These data suggest that WMV 2 and SMV-N may be strains of the same virus.

Amino Acid Sequence↗
PubMed1989

Characterization of cDNA clones coding for muscle tropomyosin of the nematode Trichostrongylus colubriformis.

The host-protective antigen from detergent-solubilised extracts of the sheep intestinal helminth Trichostrongylus colubriformis has been identified as tropomyosin. Complementary DNA clones coding for T. colubriformis muscle tropomyosin have been isolated and characterised as the first step in obtaining recombinant protein to carry out more extensive vaccination trials. The clones represent an mRNA of 1544 bases, including a relatively long 5' untranslated sequence of 307 bases and a 3' non-coding region of 344 bases. The mRNA codes for a highly alpha-helical protein of 284 residues with a molecular weight of 33,000; characteristics typically observed for the muscle tropomyosins of higher organisms. The T. colubriformis protein has 58% sequence identity with rabbit and Drosophila melanogaster muscle tropomyosins, and the differences in the protein sequence are randomly distributed throughout the molecule. There is complete identity between the three sequences for the N-terminal 9 residues, the region believed to be essential for the polymerisation of tropomyosin molecules and for binding to actin and troponin.

Amino Acid Sequence↗
PubMed1989

The keratin BIIIB gene family: isolation of cDNA clones and structure of a gene and a related pseudogene.

The nucleotide sequence of cDNA clones encoding the three major BIIIB high-sulfur wool keratin proteins (BIIIB2, 3, and 4) and the structure of a BIIIB4 gene and a BIIIB3 pseudogene are reported. Although Southern blot analysis indicates that the BIIIB genes comprise a multigene family in the sheep genome, they are poorly represented in genomic DNA libraries. The family sequence homology of the coding region extends into the 5' and 3' untranslated regions and the near 5' flanking region of the BIIIB3 and 4 genes. These homologies suggest that the BIIIB3 and 4 genes represent the latest gene duplication event in the evolution of the BIIIB multigene family. Like the genes coding for other wool keratin matrix protein components, the BIIIB genes have the conserved 18-bp sequence immediately 5' to the initiation codon and also appear to lack introns.

Amino Acid Sequence↗
PubMed1989

The use of 3' non-coding nucleotide sequences in the taxonomy of potyviruses: application to watermelon mosaic virus 2 and soybean mosaic virus-N.

The sequence of the 3' 1106 nucleotides of the watermelon mosaic virus 2 (WMV 2) genome has been determined. The sequence contains the complete coding region of the viral coat protein followed by a 3' untranslated sequence of 251 nucleotides. When these sequences were compared with the equivalent regions of the N strain of soybean mosaic virus (SMV-N), the coat protein coding regions were 82% homologous, whereas the 3' untranslated sequences were 78% homologous. Optimal alignment of the 3' untranslated regions of RNA from 13 strains of seven other distinct potyviruses revealed that the degree of homology between strains was in the range 83 to 99%. In contrast, the sequences from distinct viruses had identities in the range 39 to 53%, comparable to the level of identity found between the 3' non-coding regions of viruses from unrelated plant virus groups. On the basis of these results, WMV 2 and SMV-N could be regarded as strains of one virus. These results also suggest that the sequence of the 3' untranslated region of the potyvirus genome may be an accurate marker of genetic relatedness and could serve as an aid to identification and classification of potyviruses.

Amino Acid Sequence↗
PubMed1980

Changes in the matrix proteins of wool and mouse hair following the administration of depilatory compounds.

After sheep were defleeced with mimosine, cyclophosphamide or N-[5-(4-aminophenoxy)pentyl]-phthalimide, the first samples of the new growth of wool differed markedly in composition from the pretreatment samples, there being substantial reductions in the high-tyrosine proteins and increases in the high-sulfur proteins. Similar results were obtained with mice dehaired with mimosine and with sheep treated with low levels of mimosine which resulted in weakened wool rather than depilation. The composition of later samples of the regrowth wool showed progressive changes with time. The high-tyrosine proteins tended to approach the pretreatment levels, although this may take up to 12 weeks to occur, whereas the levels of high-sulfur proteins, after the initial increase, often fell below normal. In experiments involving defleecing with cyclophosphamide, the level of the latter proteins was still below normal after 3 months. The possibility that this altered protein composition of keratin fibres is characteristic of that portion of fibre first produced by a new or regenerating follicle was investigated in sheep and mice. It was found that wool follicles regenerating after plucking, and newly operating follicles in young sheep and mice, also produced wool and hair with a reduced content of high-tyrosine proteins. It is suggested, therefore, that the apparent long-term inhibition of the high-tyrosine proteins may not be the direct consequence of the administration of the chemical but rather be characteristic of normal wool and hair regrowth. Infusion of an amino acid mixture lacking methionine into the abomasum of sheep caused the growth of weak wool but did not suppress the synthesis of the high-tyrosine proteins. This is in contrast with previous findings that treatments which weaken wool also suppress high-tyrosine proteins.

Abomasum↗
PubMed1977

Determination of protein molecular weights in denaturing solvents using glyceryl-CPG.

Glyceryl-CPG is controlled-pore glass whose surface has been chemically modified to block its slight negative charge in aqueous solution. In contrast to normal controlled-pore glass, glyceryl-CPG can be used successfully for gel filtration of proteins in a variety of denaturing solvents, viz., 8 M urea, 6 M guanidine hydrochloride, and 0.1% sodium dodecyl sulphate. It has been found that glass with a mean pore diameter near 35 nm is suitable for the molecular weight range 17,000-100,000. Glyceryl-CPG with a smaller pore diameter is more satisfactory for molecular weights below 30,000. The stable pore size and bed dimensions of controlled-pore glass allows comparison of the conformation of a particular protein in different solvents to be made with the same column.

Chromatography, Gel↗
PubMed1976

The proteins of the keratin component of bird's beaks.

Birds' beaks have an outer shell of hard keratin which consists almost entirely of proteins which are very rich in glycine [about 30 residues per 100 residues (residues %)], contain moderate levels of tyrosine and serine (each about 8 residues %), and which have relatively low contents of cystine (about 2-5 residues %), lysine, histidine, isoleucine and methionine. Major protein fractions in the S-carboxymethyl form isolated from the beaks of six different orders of birds have similar amino acid compositions, isoelectric points (pH 4-2-4-9) and molecular weights (13,000-14,500). Detailed chromatographic electrophoretic and compositional studies of the proteins of kookaburra beak reveal them to be a family of closely related proteins with only limited heterogeneity, in contrast to mammalian keratin systems. The major kookaburra beak fraction is similar in overall composition and molecular weight to fowl epidermal scale, kookaburra claw and turtle scute proteins and shows some resemblance to reptile claw protein. Beaks also contain small amounts of protein which are distinctly different from the major fraction but which resemble feather keratin proteins in composition and size.

Amino Acids↗
PubMed1975

Controlled pore glass chromatography of protein-sodium dodecyl sulphate complexes.

The inclusion of urea has been found to eliminate adsorption of protein-sodium dodecyl sulphate (SDS) complexes to controlled pore glass. Using buffer containing 6 M urea, 0.5% SDS and glass with pore diameter 12.3 nm, it is possible to determine protein molecular weights in the range 3500-12,000. Results with glass of larger pore diameter (25.5 nm) are similar to those reported in the absence of urea in the molecular-weight range 12,000-140,000. Controlled pore glass chromatography also permits the study of the relative importance of conformation free of charge effects for those proteins which deviate from the normal calibration curve for SDS-polyacrylamide gels.

Adsorption↗
PubMed1975

Studies on the inhibition of synthesis of the tyrosine-rich proteins of wool.

Three treatments known to produce weak wool were imposed on sheep, and the effects on the synthesis of high-tyrosine wool proteins were noted. The treatments were: intravenous infusion of the amino acid mimosine (a potential chemical defleecing agent), intravenous injection of the synthetic steroid Opticortenol (dexamethasone-21-trimethylacetate), and the abomasal infusion of methionine into sheep consuming a diet of wheat. All three treatments caused a partial suppression of high-tyrosine protein synthesis. The inhibition caused by mimosine could not be prevented by the simultaneous infusion of tyrosine or phenylalanine, suggesting that in this system mimosine is not acting as a tyrosine antagonist. The role of phenylalanine in controlling the synthesis of the high-tyrosine proteins in wool was also investigated. Although the infusion of an amino acid mixture minus phenylalanine reduces the level of these proteins, supplements of phenylalanine or tyrosine do not stimulate their synthesis, irrespective of the initial level in the fibre. The improtance of aromatic amino acids in the regulation of the high-tyrosine proteins is therefore uncertain. Suppression of the high-tyrosine proteins is usually accompanied by a stimulation in the synthesis of the ultra-high-sulphur proteins, although there does not seem to be a simple stoichiometric relationship between the two protein types.

Amino Acids↗