Murine Asb-17 expression during mouse testis development and spermatogenesis

In this study we isolated a murine mAsb-17 from mouse testis by RT-PCR using primers designed based on the sequences from the GenBank database. The sequence analysis showed that mAsb-17 encodes a 295 amino acid polypeptide with a molecular weight of approximately 34 kDa containing two ankyrin repeats and one SOCS box. The amino acid sequence of mASB-17 showed 87.5%, 98.3% and 92.9% identity with that of human, rat and dog, respectively. Interestingly, northern blot analysis showed that mAsb-17 was expressed only in the testis. The expression analysis by RT-PCR for mAsb-17 in mouse indicates that mAsb-17 is expressed from the fourth week after birth to adult, with the highest expression in round spermatids. Both northern blot and RT-PCR analyses suggest that mASB-17 may play essential roles in testis development and spermatogenesis.

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The purification and N-terminal amino acid sequence analysis of the high molecular weight gluten polypeptides of wheat

Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology ◽

10.1016/0167-4838(84)90293-0 ◽

1984 ◽

Vol 788 (1) ◽

pp. 23-34 ◽

Cited By ~ 70

Author(s):

Peter R. Shewry ◽

J.Michael Field ◽

Audrey J. Faulks ◽

Saroj Parmar ◽

Benjamin J. Miflin ◽

...

Keyword(s):

Molecular Weight ◽

Amino Acid ◽

Sequence Analysis ◽

Amino Acid Sequence ◽

High Molecular Weight ◽

Amino Acid Sequence Analysis ◽

Terminal Amino Acid ◽

Terminal Amino ◽

Terminal Amino Acid Sequence

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Direct evidence for methylation of arginine residues in high molecular weight forms of basic fibroblast growth factor.

Cell Regulation ◽

10.1091/mbc.2.2.87 ◽

1991 ◽

Vol 2 (2) ◽

pp. 87-93 ◽

Cited By ~ 34

Author(s):

W H Burgess ◽

J Bizik ◽

T Mehlman ◽

N Quarto ◽

D B Rifkin

Keyword(s):

Molecular Weight ◽

Amino Acid ◽

Growth Factor ◽

Sequence Analysis ◽

Amino Acid Sequence ◽

Fibroblast Growth Factor ◽

High Molecular Weight ◽

Fibroblast Growth ◽

Amino Acid Sequence Analysis ◽

Arginine Residues

Basic fibroblast growth factor (bFGF) is a heparin-binding angiogenic polypeptide mitogen. Protein sequence analysis of bFGF isolated from tissue sources initially established that it is composed of 146 amino acids (apparent Mr 18,000). More recently larger apparent molecular weight forms have been identified and partially characterized. In addition, these high molecular weight forms (apparent Mr 22,000 and 25,000) have been shown to localize preferentially to nuclear fractions of transfected cells. In this report we demonstrate that the higher molecular weight, amino terminally extended forms of bFGF contain methylated arginine residues. The demonstration is based on 1) amino acid sequence analysis of a protein known to contain methylated arginine (myelin basic protein) and a comparison with amino acid sequence analysis of trypsin-derived fragments of the high molecular weight bFGF purified from guinea pig brain and 2) the ability to label in vivo the high molecular weight forms of bFGF with S-adenosyl-L-(methyl-3H)-methionine, the substrate of arginine-protein methylase I. These results are suggestive of a role of arginine methylation in directing nuclear localization of certain forms of bFGF.

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Aldehyde dehydrogenase from adult human brain that dehydrogenates γ-aminobutyraldehyde: purification, characterization, cloning and distribution

Biochemical Journal ◽

10.1042/bj3160317 ◽

1996 ◽

Vol 316 (1) ◽

pp. 317-324 ◽

Cited By ~ 20

Author(s):

Alexandra KIKONYOGO ◽

Regina PIETRUSZKO

Keyword(s):

Amino Acid ◽

Amino Acid Sequence ◽

Human Brain ◽

Aldehyde Dehydrogenase ◽

Northern Blot ◽

Blot Analysis ◽

Northern Blot Analysis ◽

Mrna Levels ◽

Adult Human Brain ◽

Adult Human

Enzyme purification and characterization, cDNA cloning and Northern blot analysis were the techniques utilized during this investigation to determine the identity and occurrence of the aldehyde dehydrogenase that metabolizes γ-aminobutyraldehyde in adult human brain. The purification yielded one major protein which was active with γ-aminobutyraldehyde. It had the physicochemical and kinetic properties of the human liver E3 isoenzyme of aldehyde dehydrogenase (EC 1.2.1.3), and also interacted with an anti-(liver E3 isoenzyme) antibody. Tryptic peptides derived from the purified brain protein matched the amino acid sequence of the liver E3 isoenzyme. Employing liver E3 cDNA, a human cerebellar cDNA library was screened and a 2.0 kb cDNA fragment was isolated. The cerebellar cDNA yielded a derived primary structure which differed from the liver E3 amino acid sequence by a single serine-to-cysteine substitution at position 88 (position 84 in the liver sequence). Thus the γ-aminobutyraldehyde-metabolizing enzyme from human brain can be identified as E3′, a variant of the E3 isoenzyme. The catalytic properties of the brain variant were indistinguishable from those of E3, and so the functional importance of this variant is at present unknown. The distribution of this enzyme in brain was investigated by Northern blot analysis, which demonstrated the presence of E3′ mRNA in all regions of the human brain. mRNA levels were variable in the different brain areas, with the highest levels in the spinal cord and the lowest in the occipital pole.

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Structure of an ovine interferon receptor and its expression in endometrium

Journal of Molecular Endocrinology ◽

10.1677/jme.0.0170207 ◽

1996 ◽

Vol 17 (3) ◽

pp. 207-215 ◽

Cited By ~ 11

Author(s):

S Kaluz ◽

P A Fisher ◽

M Kaluzova ◽

E L Sheldrick ◽

A P F Flint

Keyword(s):

Amino Acid ◽

Northern Blot ◽

Northern Blot Analysis ◽

Type I Interferon ◽

Transmembrane Protein ◽

Type I ◽

Rt Pcr ◽

Pcr Product ◽

Interferon Receptor

ABSTRACT A sheep type I interferon receptor (oIFNAR1) cDNA was isolated from a λ-ZAP library using a reverse transcription (RT)-PCR product probe generated from oestrous endometrial RNA. The oIFNAR1 cDNA was 79, 66 and 95% homologous to human, murine and bovine IFNAR1 cDNAs respectively. The encoded receptor was a 560-amino acid transmembrane protein 80, 66 and 95% similar to human, murine and bovine IFNAR1 respectively. Northern blot analysis of endometrial mRNA revealed the presence of 6·5, 4·3 and 3·7 kb transcripts. Using semi-quantitative RT-PCR the oIFNAR1 mRNA was not found to be down-regulated after 72 h treatment with bovine recombinant IFN-αI in in vitro experiments with endometrial explants.

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Isolation and Structural Charaderization of a Potent Inhibitor of Coagulation Factor Xa from the Leech Haementeria ghilianii

Thrombosis and Haemostasis ◽

10.1055/s-0038-1646610 ◽

1989 ◽

Vol 61 (03) ◽

pp. 437-441 ◽

Cited By ~ 28

Author(s):

Cindra Condra ◽

Elka Nutt ◽

Christopher J Petroski ◽

Ellen Simpson ◽

P A Friedman ◽

...

Keyword(s):

Molecular Weight ◽

Salivary Gland ◽

Amino Acid ◽

Amino Acid Sequence ◽

Western Blot ◽

Potent Inhibitor ◽

Factor Xa ◽

Coagulation Factor ◽

Sds Page ◽

Bovine Factor

SummaryThe present work reports the discovery and charactenzation of an anticoagulant protein in the salivary gland of the giant bloodsucking leech, H. ghilianii, which is a specific and potent inhibitor of coagulation factor Xa. The inhibitor, purified to homogeneity, displayed subnanomolar inhibition of bovine factor Xa and had a molecular weight of approximately 15,000 as deduced by denaturing SDS-PAGE. The amino acid sequence of the first 43 residues of the H. ghilianii derived inhibitor displayed a striking homology to antistasin, the recently described subnanomolar inhibitor of factor Xa isolated from the Mexican leech, H. officinalis. Antisera prepared to antistasin cross-reacted with the H. ghilianii protein in Western Blot analysis. These data indicate that the giant Amazonian leech, H. ghilianii, and the smaller Mexican leech, H. officinalrs, have similar proteins which disrupt the normal hemostatic clotting mechanisms in their mammalian host’s blood.

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Complete Covalent Structure of Human Platelet Factor 4

Thrombosis and Haemostasis ◽

10.1055/s-0038-1657071 ◽

1979 ◽

Vol 42 (05) ◽

pp. 1652-1660 ◽

Cited By ~ 4

Author(s):

Francis J Morgan ◽

Geoffrey S Begg ◽

Colin N Chesterman

Keyword(s):

Amino Acids ◽

Molecular Weight ◽

Amino Acid ◽

Amino Acid Sequence ◽

Human Platelet ◽

Platelet Factor 4 ◽

Platelet Factor ◽

Disulphide Bonds ◽

Covalent Structure

SummaryThe amino acid sequence of the subunit of human platelet factor 4 has been determined. Human platelet factor 4 consists of identical subunits containing 70 amino acids, each with a molecular weight of 7,756. The molecule contains no methionine, phenylalanine or tryptophan. The proposed amino acid sequence of PF4 is: Glu-Ala-Glu-Glu-Asp-Gly-Asp-Leu-Gln-Cys-Leu-Cys-Val-Lys-Thr-Thr-Ser- Gln-Val-Arg-Pro-Arg-His-Ile-Thr-Ser-Leu-Glu-Val-Ile-Lys-Ala-Gly-Pro-His-Cys-Pro-Thr-Ala-Gin- Leu-Ile-Ala-Thr-Leu-Lys-Asn-Gly-Arg-Lys-Ile-Cys-Leu-Asp-Leu-Gln-Ala-Pro-Leu-Tyr-Lys-Lys- Ile-Ile-Lys-Lys-Leu-Leu-Glu-Ser. From consideration of the homology with p-thromboglobulin, disulphide bonds between residues 10 and 36 and between residues 12 and 52 can be inferred.

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Identification of the gene encoding 3-(5-oxo-2-thioxoimidazolidin-4-yl) propionic acid desulfhydrase in Burkholderia sp. HME13

Bioscience Biotechnology and Biochemistry ◽

10.1093/bbb/zbaa066 ◽

2020 ◽

Vol 85 (3) ◽

pp. 626-629

Author(s):

Hisashi Muramatsu ◽

Hiroki Maguchi ◽

Taisuke Harada ◽

Takehiro Kashiwagi ◽

Chul-Sa Kim ◽

...

Keyword(s):

Amino Acid ◽

Sequence Analysis ◽

Amino Acid Sequence ◽

Propionic Acid ◽

Unknown Function ◽

Protein Family ◽

Amino Acid Sequence Analysis ◽

Gene Encoding

ABSTRACT Here, we report the identification of the gene encoding a novel enzyme, 3-(5-oxo-2-thioxoimidazolidin-4-yl) propionic acid desulfhydrase, in Burkholderia sp. HME13. The enzyme converts 3-(5-oxo-2-thioxoimidazolidin-4-yl) propionic acid and H2O to 3-(2,5-dioxoimidazolidin-4-yl) propionic acid and H2S. Amino acid sequence analysis of the enzyme indicates that it belongs to the DUF917 protein family, which consists of proteins of unknown function.

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