Search

Your search keyword '"Cederlund, Ella"' showing total 35 results
Start Over Author "Cederlund, Ella"
35 results on '"Cederlund, Ella"'

5. Novel long-chain neurotoxins from Bungarus candidus distinguish the two binding sites in muscle-type nicotinic acetylcholine receptors

Author

Utkin, Yuri N., primary, Kuch, Ulrich, additional, Kasheverov, Igor E., additional, Lebedev, Dmitry S., additional, Cederlund, Ella, additional, Molles, Brian E., additional, Polyak, Iakov, additional, Ivanov, Igor A., additional, Prokopev, Nikita A., additional, Ziganshin, Rustam H., additional, Jornvall, Hans, additional, Alvelius, Gunvor, additional, Chanhome, Lawan, additional, Warrell, David A., additional, Mebs, Dietrich, additional, Bergman, Tomas, additional, and Tsetlin, Victor I., additional

Published
2019
Full Text
View/download PDF

7. Systemic AA amyloidosis in the red fox (Vulpes vulpes)

Author

Rising, Anna, Cederlund, Ella, Palmberg, Carina, Uhlhorn, Henrik, Gaunitz, Stefan, Nordling, Kerstin, Ågren, Erik, Ihse, Elisabet, Westermark, Gunilla T., Tjernberg, Lars, Jörnvall, Hans, Johansson, Jan, and Westermark, Per

Subjects
Male, Sweden, Serum Amyloid A Protein, Sequence Homology, Amino Acid, animal diseases, Foxes, Gene Expression, Amyloidosis, Kidney, Mice, parasitic diseases, For the Record, Epidemiological Monitoring, Animals, Female, Amino Acid Sequence, Sequence Alignment, Spleen
Abstract

Amyloid A (AA) amyloidosis occurs spontaneously in many mammals and birds, but the prevalence varies considerably among different species, and even among subgroups of the same species. The Blue fox and the Gray fox seem to be resistant to the development of AA amyloidosis, while Island foxes have a high prevalence of the disease. Herein, we report on the identification of AA amyloidosis in the Red fox (Vulpes vulpes). Edman degradation and tandem MS analysis of proteolyzed amyloid protein revealed that the amyloid partly was composed of full-length SAA. Its amino acid sequence was determined and found to consist of 111 amino acid residues. Based on inter-species sequence comparisons we found four residue exchanges (Ser31, Lys63, Leu71, Lys72) between the Red and Blue fox SAAs. Lys63 seems unique to the Red fox SAA. We found no obvious explanation to how these exchanges might correlate with the reported differences in SAA amyloidogenicity. Furthermore, in contrast to fibrils from many other mammalian species, the isolated amyloid fibrils from Red fox did not seed AA amyloidosis in a mouse model.

Published
2017

8. Systemic AA amyloidosis in the red fox (Vulpes vulpes)

Author

Rising, Anna, primary, Cederlund, Ella, additional, Palmberg, Carina, additional, Uhlhorn, Henrik, additional, Gaunitz, Stefan, additional, Nordling, Kerstin, additional, Ågren, Erik, additional, Ihse, Elisabet, additional, Westermark, Gunilla T., additional, Tjernberg, Lars, additional, Jörnvall, Hans, additional, Johansson, Jan, additional, and Westermark, Per, additional

Published
2017
Full Text
View/download PDF

23. Activity of the plant peptide aglycin in mammalian systems.

Author

Xin-Peng Dun, Jian-He Wang, Lei Chen, Jie Lu, Fa-Fang Li, Yan-Ying Zhao, Cederlund, Ella, Bryzgalova, Galina, Efendic, Suad, Jörnvall, Hans, Zheng-Wang Chen, and Bergman, Tomas

Subjects
PEPTIDES, PLANT proteins, PLANT polymers, MAMMALS, PEPSIN, TRYPSIN
Abstract

A 37 residue peptide, aglycin, has been purified from porcine intestine. The sequence is identical to that of residues 27–63 of plant albumin 1 B precursor (PA1B, chain b) from pea seeds. Aglycin resists in vitro proteolysis by pepsin, trypsin and Glu-C protease, compatible with its intestinal occurrence and an exogenous origin from plant food. When subcutaneously injected into mice (at 10 µg·g−1 body weight), aglycin has a hyperglycemic effect resulting in a doubling of the blood glucose level within 60 min. Using surface plasmon resonance biosensor technology, an aglycin binding protein with an apparent molecular mass of 34 kDa was detected in membrane protein extracts from porcine and mice pancreas. The polypeptide was purified by affinity chromatography and identified through peptide mass fingerprinting as the voltage-dependent anion-selective channel protein 1. The results indicate that aglycin has the potential to interfere with mammalian physiology. [ABSTRACT FROM AUTHOR]

Published
2007
Full Text
View/download PDF

26. Primary structure of glycolate oxidase from spinach.

Author

Cederlund, Ella, Lindqvist, Ylva, Söderlund, Gustaf, Bränden, Carl-Ivar, and Jörnvall, Hans

Subjects
*OXIDASES, *SPINACH, *PROTEINS, *AMINO acids, *AMINO acid sequence, *ORGANIC acids, *METHIONINE, *HOMOLOGY (Biology)
Abstract

The primary structure of glycolate oxidase from spinach has been determined. Six different types of peptide digest were investigated, utilizing CNBr, proteolytic enzymes, and chemical modifications to change a specificity of cleavage. In total, 90 peptides were purified and analyzed. The studies were aimed at correlation with crystallographic analysis of the same protein carried through in parallel and with eDNA studies which utilized initially determined amino acid sequences for synthesis of oligonucleotide probes. Continuous comparisons with the results from the crystallographic studies helped at an early stage to secure peptide overlaps, at the same time as the peptide data secured residue assignments in the electron density maps. In the end, all data agree and regions from all parts of the molecule have been checked by independent methods of analysis. The primary structure establishes the type of N-terminal post-translational processing, and yields information on segments not fully defined in electron density maps. Combined, the chemical, crystallographic, and eDNA data give extensive reliability. The peptide analysis shows that the N-terminus is blocked by acylation of the initiator methionine, which is in a primary structure typical for non-removal of the methionine in the processing events of the nascent protein chain. The molecule is comparatively rich in menthionine and some other generally less common residues, but has only one cysteine residue and no extensive hydrophobic segment. An amino acid sequence homology with flavocytochrome b2 from yeast, as expected from known similarities in tertiary structure, is observed (33% residue identities). [ABSTRACT FROM AUTHOR]

Published
1988
Full Text
View/download PDF

27. Sorbitol dehydrogenase.

Author

Jeffery, Jonathan, Cederlund, Ella, and Jörnvall, Hans

Subjects
*SORBITOL, *POLYOLS, *DEHYDROGENASES, *ALCOHOL dehydrogenase, *ENZYMES
Abstract

The first primary structure for a sorbitol dehydrogenase has been determined by analysis of the tetrameric enzyme from sheep liver. The [14C]carboxymethylated protein was cleaved with CNBr and proteolytic enzymes. Peptides were purified by several methods, often utilizing exclusion chromatography for pre-fractionation and reverse-phase high-performance liquid chromatography for final purification. Different methods of sequence analysis complemented each other, mainly the manual dimethylaminoazobenzene isothiocyanate method and the use of liquid-phase sequencer degradations. All eight major CNBr fragments were purified and form the basis of the work. Three minor CNBr fragments derived from an acid cleavage and from a partly resistant Met-Thr bond were also obtained, as well as evidence for a contaminating homologous polypeptide. Most of the tryptic peptides were purified, including all with methionine residues, thus overlapping the CNBr fragments. Combined, all data permit the deduction of a 354-residue amino acid sequence for the polypeptide chain of sorbitol dehydrogenase. The N terminus is acyl-blocked, the C terminus is formed by a prohne residue, tryptophan is the least common residue (two, at positions 50 and 301) and there are 10 cysteine residues, including the residue previously shown to be especially reactive (at postion 43). Similarities to 'long' alcohol dehydrogenases have functional implications. [ABSTRACT FROM AUTHOR]

Published
1984
Full Text
View/download PDF

28. Characterization of a marsupial glutathione transferase, a class Alpha enzyme from Brown Antechinus (Antechinus stuartii) 1The sequence reported in this paper has been deposited in the SWISS-PROT data base (accession no. P80894).1

Author

Bolton, Robyn M, Curstedt, Linda, Cederlund, Ella, Hjelmqvist, Lars, Mannervik, Bengt, Ahokas, Jorma T, and Jörnvall, Hans

Subjects
Amino acid sequence, Molecular evolution, Enzyme family, Cytosolic glutathione transferase, Structure–function relationship
Abstract

The major form of glutathione transferase from the marsupial Antechinus stuartii has been purified and characterized as an Alpha class enzyme (AstGSTA1-1) with distant sequence relationships to other class Alpha sublines, compatible with the early origin of marsupials. Amino acid replacements toward the closest enzyme characterized (chicken, form A3) involve no less than 79 positions (36%). At the active site, as deduced from comparisons with the known tertiary structure of the corresponding human enzyme, over half of the residues (8 of 15) ascribed to substrate binding interactions are exchanged although the general character of that site is conserved, while only 1 of 11 positions ascribed to interactions with GSH is exchanged. Class variability and species variability appear to coincide, with divergent segments centering around positions 33–49, 103–130 and 205–222. The pattern is reminiscent of that in similarly multiple MDR alcohol dehydrogenases. Both these enzyme families involved in cellular defense reactions have diverged considerably.

Full Text
View/download PDF

29. Peptides of postulated inhibin activity

Author

Kohan, Sergio, Fröysa, Berit, Cederlund, Ella, Fairwell, Thomas, Lerner, Richard, Johansson, Jan, Khan, Shafiq, Ritzen, Martin, Jörnvall, Hans, Cekan, Sten, and Diczfalusy, Egon

Abstract

A 94-residue polypeptide isolated from human seminal plasma and its chemically synthesized C-terminal 28-residue segment were studied in an in vitro inhibin bioassay utilizing rat pituitary cell cultures. Both peptides have previously been claimed to have inhibin activities, and the effects on the secretion and cellular content of gonadotrophins (FSH and LH) were now assessed in the in vitro assay. No inhibition was found. After 72 h of culture, both the cellular content and the spontaneous as well as the LHRH-stimulated release of bioactive or immunoactive FSH and LH remained unaffected. Similarly, no effects were found on the storage and/or release of prolactin, growth hormone, or thyrotropin. We conclude that both the native 94-residue peptide and the synthetic replicate of its C-terminal 28-residue segment, do not influence the pituitary FSH secretion when assessed in this in vitro system.

Published
1986
Full Text
View/download PDF

30. Analysis of an inhibin preparation reveals apparent identity between a peptide with inhibin-like activity and a sperm-coating antigen

Author

Johansson, Jan, Sheth, Anil, Cederlund, Ella, and Jörnvall, Hans

Abstract

The amino acid sequence of a large form of inhibin-like peptide in human seminal plasma was determined, and compared with structures reported for similar inhibin preparations and a seminal plasma globulin. The data confirm and correlate previous reports on this form of inhibin-like peptide. The structural comparisons further suggest that the peptide is closely similar to or possibly identical to a sperm-coating antigen reported to be synthesized from prostatic epithelium. This may correlate with non-gonadal origins of inhibin-like material and will help to elucidate the biological roles of inhibin(s).

Published
1984
Full Text
View/download PDF

31. 11‐Hydroxythromboxane B2dehydrogenase is identical to cytosolic aldehyde dehydrogenase

Author

Westlund, Pär, Fylling, Ann Catrin, Cederlund, Ella, and Jörnvall, Hans

Abstract

11 ‐Hydroxythromboxane B2dehydrogenase purified from porcine kidney has been identified as cytosolic aldehyde dehydrogenase (EC 1.2.1.3). This identification is based on protein characteristics, sequence analysis of one proteolytic digest, blocked N‐terminus, subunit molecular mass of 55 kDa, and enzymatic activities. The sequence difference with the human enzyme is 7.5% in the fragments analyzed (29 exchanges of 388 positions, corresponding to the expected species variability for cytosolic aldehyde dehydrogenase The substrate thromboxane B2contains a hemiacetal in its ring structure, but the reaction most likely proceeds via the aldehyde form of the substrate. This finding is in agreement with the proposed metabolism of 4‐hydroxycyclophosphamide and highlights the possibility that molecules containing a hemiacetal structure can function as substrates for aldehyde dehydrogenase.

Published
1994
Full Text
View/download PDF

32. Acetyl xylan esterase II from Penicillium purpurogenumis similar to an esterase from Trichoderma reeseibut lacks a cellulose binding domain

Author

Gutiérrez, Rodrigo, Cederlund, Ella, Hjelmqvist, Lars, Peirano, Alessandra, Herrera, Francisco, Ghosh, Debashis, Duax, William, Jörnvall, Hans, and Eyzaguirre, Jaime

Abstract

Penicillium purpurogenumproduces at least two acetyl xylan esterases (AXE I and II). The AXE II cDNA, genomic DNA and mature protein sequences were determined and show that the axe 2gene contains two introns, that the primary translation product has a signal peptide of 27 residues, and that the mature protein has 207 residues. The sequence is similar to the catalytic domain of AXE I from Trichoderma reesei(67% residue identity) and putative active site residues are conserved, but the Penicilliumenzyme lacks the linker and cellulose binding domain, thus explaining why it does not bind cellulose in contrast to the Trichodermaenzyme. These results point to a possible common ancestor gene for the active site domain, while the linker and the binding domain may have been added to the Trichodermaesterase by gene fusion.

Published
1998
Full Text
View/download PDF

35. C‐Terminal Sequence Analysis

Author

Bergman, Tomas, Cederlund, Ella, Jörnvall, Hans, and Fowler, Elizabeth

Abstract

Carboxy‐terminal (C‐terminal) sequence analysis is used for direct confirmation of the C‐terminal sequence of native and expressed proteins, for detection and characterization of protein processing at the C‐terminus, for identification of post‐translational proteolytic cleavages, and for obtaining partial sequence information on N‐terminally blocked protein samples in order to facilitate design of oligonucleotide probes for gene cloning. This unit describes an automated chemical method and a manual enzymatic (carboxypeptidase digestion) method for determining C‐terminal sequence information. Carboxypeptidase digestion requires only a standard amino acid analysis method.

Published
2003
Full Text
View/download PDF

Catalog

Books, media, physical & digital resources
See catalog results