PubMed Health⌕ Search

Biomedical subjects

S Odani

Publications and source records attributed to S Odani.

At least 73 records · Page 4Linked to original sources
PubMed1986

The heparin-binding site(s) of histidine-rich glycoprotein as suggested by sequence homology with antithrombin III.

A high degree of sequence homology has been found between the N-terminal region of histidine-rich glycoprotein (HRG) and that of antithrombin III (AT III) where the putative heparin-binding site of AT III is located. The amino acid residue at the position corresponding to Arg-47 of AT III that is essential for the heparin-binding was also arginine (Arg 23 and 78) in the homologous sequences of HRG. These observations strongly suggest that the heparin-binding sites of HRG and AT III are evolutionarily related. There was no apparent sequence similarity between the remaining about 70% portions of the two proteins.

Amino Acid Sequence↗
PubMed1986

Amino acid sequence of the variable region of heavy chain in immunoglobulin (Mot) having unusual papain cleavage sites.

An IgGl(lambda) Mot myeloma protein showed a unique susceptibility toward papain digestion. The Fab fragment of Mot was more digestible with papain than the Fc fragment. This phenomenon was found to occur by unusual cleavage of the Fd fragment with papain. Determination of the complete primary structure of the V region of the H chain of Mot identified two papain cleavage sites in the second complementarity-determining region (CDR). Amino acid sequence of the cleavage sites was Ser(55)-Asp-Asp-Argdecrease-Thr-Thr-Tyr-Gly-Pro-Argdecrease- Ser-Gln- (decrease = cleavage site). In the vicinity of these cleavage sites, many hydrophilic and polar residues are present and the predicted secondary structure near these cleavage sites suggested that this region was exposed on the surface of the molecule, and that the unusual papain cleavage of the IgG Mot might be caused by a unique conformation of the molecule, making it highly susceptible to enzyme digestion.

Amino Acid Sequence↗
PubMed1986

Beta 2-microglobulin: a new form of amyloid protein associated with chronic hemodialysis.

Carpal tunnel syndrome (CTS) has been associated with amyloid deposits and is now regarded as a major complication in chronic hemodialysis patients. While this new syndrome has been receiving increasing attention, its etiology has not been clarified. We have isolated amyloid fibrils from amyloid laden tissues inside the carpal tunnel in four different hemodialysis patients with CTS. After solubilization in guanidine HCl, a significant amount of the protein was located in a homogeneous, low molecular weight fraction. Each protein was found to be identical to beta 2-microglobulin with regard to its molecular weight of 11,000 on SDS-PAGE, amino acid composition and N-terminal amino acids: Ile-Gln-Arg-Thr-Pro-Lys-Ile-Gln-Val-Tyr-Ser-Arg-His-Pro-Ala-Glu. In direct immunofluorescent study, anti-beta 2-microglobulin did react positively with amyloid deposits. These results demonstrate that the amyloid associated with chronic hemodialysis contains as major component a new form of amyloid fibril protein that is homologous to beta 2-microglobulin. It is postulated that beta 2-microglobulin cannot be removed from the blood by conventional hemodialysis, and accumulates in tissues causing the formation of amyloid fibrils, which, having a relatively high affinity to the carpal tunnel area, thus causes CTS.

Amino Acids↗
PubMed1986

Wheat germ trypsin inhibitors. Isolation and structural characterization of single-headed and double-headed inhibitors of the Bowman-Birk type.

A number of trypsin inhibitors were isolated from wheat germs by affinity chromatography on immobilized trypsin, gel-filtration, and ion-exchange and reverse-phase chromatography. These inhibitors were classified into two groups, inhibitors I (Mr = 14,500) and II (Mr = 7,000), based on their molecular sizes. Inhibitors I and II inhibited bovine trypsin stoichiometorically at an enzyme to inhibitor ratio of 2 and 1, respectively. Sequence analysis of these inhibitors indicated a high degree of homology and that inhibitors I had a duplicated structure of inhibitors II. They are highly homologous to double-headed proteinase inhibitors (Bowman-Birk inhibitors) of Leguminosae plants. Inhibitors II are the first example of single-headed inhibitor corresponding to one inhibitory domain of the Bowman-Birk type double-headed inhibitors, which suggests that inhibitors II are relic of an ancestral single-headed inhibitor before the gene-duplication that led to the formation of present-day Bowman-Birk type inhibitors.

Amino Acid Sequence↗
PubMed1985

A new form of amyloid protein associated with chronic hemodialysis was identified as beta 2-microglobulin.

Amyloid fibrils were isolated from amyloid-laden tissue obtained from a chronic hemodialysis patient with carpal tunnel syndrome. After solubilization in guanidine HCl, a significant amount of the protein was located in a homogeneous low molecular weight fraction. The protein was found to be identical to beta 2-microglobulin, with regard to its molecular weight of 11,000, amino acid composition and 16 amino-terminal amino acids: Ile-Gln-Arg-Thr-Pro-Lys-Ile-Gln-Val-Tyr-Ser-Arg-His-Pro-Ala-Glu-. These results demonstrate that the amyloid associated with chronic hemodialysis contains as major component a new form of amyloid fibril protein that is homologous to beta 2-microglobulin.

Amino Acid Sequence↗
PubMed1985

Molecular cloning and the nucleotide sequence of cDNA for neuron-specific enolase messenger RNA of rat brain.

The cDNAs to mRNA for rat gamma gamma enolase (neuron-specific enolase; NSE; EC 4.2.1.11) were isolated from a cDNA library by using differential colony hybridization and a hybrid-selected translation assay. By overlapping of the nucleotide sequences of several cDNA inserts, it was found that they spanned 2232 base pairs (bp) which included 1299 bp of the complete coding region, 68 bp of the 5' noncoding region, and 848 bp of the 3' noncoding region, including a polyadenylylation signal. In addition, the poly(A) tail was also found. The amino acid sequence deduced from the nucleotide sequence was composed of 433 amino acids. Southern blot analysis with a cDNA insert detected one hybridizing fragment in rat genomic DNA digested with several different restriction enzymes. Dot-blot and transfer hybridization analyses of poly(A)+ RNA from developing rat brains showed an increase of NSE mRNA 10-30 days after birth.

Amino Acid Sequence↗
PubMed1985

Human histidine-rich glycoprotein: simultaneous purification with antithrombin III and characterization of its gross structure.

The simple and simultaneous purification of histidine-rich glycoprotein (HRG) and antithrombin III (AT III) from human plasma and gross structural characterization of HRG have been performed. The purification method consists of two chromatographic procedures using heparin-agarose and DEAE-Sephadex. The yields of HRG and AT III were 22 mg and 70 mg, respectively, from 1 liter of plasma. The purified HRG is a single-chain polypeptide with a molecular weight (Mr) of 75,000 on sodium dodecyl sulfate (SDS)-polyacrylamide gel electrophoresis, indicating it was the native form of this protein. Cyanogen bromide cleavage of HRG, followed by analysis of the amino acid composition and determination of the amino-terminal sequence of each purified cyanogen bromide fragment established that the gross structure of HRG consisted of three cyanogen bromide fragments; an amino-terminal CN-50 kDa fragment (Mr 50,000) and a carboxy-terminal small fragment of eight amino acids, and a CN-30 kDa fragment (Mr 30,000) between them. As to the amino acid composition of the CN-30 kDa fragment, it had an unusually high content of histidine (25 mol%), suggesting the presence of a histidine-rich region(s) in the carboxy-terminal half of the molecule. These results together with our previous results (Koide, T., Odani, S., & Ono, T. (1982) FEBS Lett. 141, 222-224) and those of Morgan (Morgan, W.T. (1985) Biochemistry 24, 1496-1501) imply that HRG is composed of at least two domains with distinct functional properties; i.e. an amino-terminal domain with heparin-binding ability and a carboxy-terminal domain with heme- and divalent metal-binding abilities.

Amino Acids↗
PubMed1984

Isolation and immunohistochemical localization of a cerebellar protein.

Our previous report described that a protein called spot 35 is found in the cerebellar cytosol of adult rats by two-dimensional gel electrophoresis. In this paper we isolated this protein from the soluble fraction of bovine and rat cerebella and then prepared an antiserum against the bovine protein. This protein shows pI around 5.3 and Mr around 27 kdalton. Determination of the amino acid composition of this protein shows high glutamic acid, aspartic acid and leucine contents. Using the antiserum we examined the immunohistochemical localization of this protein by the peroxidase-antiperoxidase method. Purkinje cells, their dendrites and axons were immunohistochemically stained in the cerebella of adult rats, rabbits and humans. Other cells, such as granule cells and glial cells, and myelin did not react to the antiserum.

Amino Acids↗
PubMed1984

Antithrombin III Toyama: replacement of arginine-47 by cysteine in hereditary abnormal antithrombin III that lacks heparin-binding ability.

Structural analyses of a hereditary abnormal antithrombin III, antithrombin III Toyama, which has normal progressive antithrombin activity but no heparin cofactor activity, have been carried out to elucidate the molecular abnormality causing recurrent thrombophlebitis of a patient and to identify an amino acid residue essential for the binding with heparin. Abnormal antithrombin III was reduced, S-pyridylethylated, and treated with cyanogen bromide. Eleven fragments were isolated by the combination of Sephadex G-50 gel filtration and reversed-phase HPLC and compared with those from normal antithrombin III. One large fragment (CN-III) that appeared to have a different amino acid composition from that of the corresponding fragment from normal antithrombin III was digested with trypsin, and the digests were separated by HPLC. The abnormal peptide was identified by comparing the peptide map with that from normal antithrombin III. Amino acid sequence analysis of the abnormal peptide indicated that the arginine-47 of normal antithrombin III had been replaced by cysteine in antithrombin III Toyama. One base mutation, C leads to T, in the 5' terminal position of the arginine-47 genetic codon (CGT) is probably responsible for this substitution. These results also suggest that arginine-47 is an essential amino acid residue for the binding with heparin.

Amino Acid Sequence↗
PubMed1983

Isolation and characterization of the three fractions (DE-I, DE-II and DE-III) of rat-liver Z-protein and the complete primary structure of DE-II.

Three fractions (DE-I, DE-II and DE-III) of Z-protein (fatty acid binding protein) have been isolated from rat liver cytosol by DEAE-cellulose chromatography and characterized. They had the same molecular weight of 14000 and essentially identical amino acid composition. However, compositions of endogenous fatty acids were found to differ strikingly from one another. Long-chain fatty acids detected in DE-II were palmitic, stearic, oleic, linoleic and arachidonic acids. In contrast to DE-II, DE-III contained mainly arachidonic acid. Molar ratios of endogenous long-chain fatty acids to both DE-II and DE-III were estimated to be around 1.0. Unlike the latter two fractions, DE-I was virtually lipid-free. Analyses of the three fractions by polyacrylamide gel electrophoresis, electrofocusing and DEAE-cellulose chromatography before and after delipidation suggested that the difference between DE-I and DE-II was in part due to fatty acids bound to DE-II. In contrast, DE-III appeared to be somewhat different from these forms in its protein structure, though tryptic peptide mappings of the three fractions did not reveal clear differences among them. Analysis of the primary structure was made on the most abundant fraction, DE-II, to investigate the relationship among the three fractions and to other proteins. The protein was a single chain consisting of 127 amino acid residues and had a mostly acetylated NH2 terminus and a free sulfhydryl group. The complete sequence of Z-protein showed striking homology to cellular retinoid binding proteins and peripheral nerve myelin P2 protein, which indicated the presence of a new family of cellular lipid-binding proteins diverged from a common ancestor. A possible intragenic duplication of Z-protein was also suggested.

Amino Acid Sequence↗
PubMed1983

Structural relationship between barley (Hordeum vulgare) trypsin inhibitor and castor-bean (Ricinus communis) storage protein.

A significant sequence homology was found between barley (Hordeum vulgare) trypsin inhibitor and castor-bean (Ricinus communis) seed glutamine-rich storage protein. This appears to suggest a divergent evolution of the two different classes of seed proteins and to support a view that plant proteinase inhibitors may also act as storage proteins.

Amino Acid Sequence↗
PubMed1983

Isolation and characterization of a hereditary abnormal antithrombin III 'Antithrombin III Toyama'.

A hereditary abnormal antithrombin III (AT-III) 'Antithrombin III Toyama' was purified from the plasma of a patient with recurrent thrombophlebitis by a procedure involving barium chloride and ammonium sulfate fractionations, affinity chromatography on anti-AT-III-Sepharose gel, and DEAE-Sephadex chromatography. Purified abnormal AT-III was shown to be the same as normal one in the molecular size, having the same molecular weight, amino-terminal sequence and carboxy-terminal amino acid. Abnormal AT-III gave the same UV spectrum as normal AT-III and both proteins were immunologically identical. Abnormal AT-III, however, showed the different electrophoretic mobility on agarose gel electrophoresis and immunoelectrophoresis. Abnormal AT-III was more electronegative than normal one, before and after a neuraminidase digestion of both proteins. These results suggest that in antithrombin III Toyama an amino acid residue at the heparin-binding site has been replaced by less basic or more acidic one which has no ability to interact with heparin, resulting in a loss of heparin cofactor activity of this protein.

Adult↗
PubMed1983

The complete amino acid sequence of barley trypsin inhibitor.

The amino acid sequence of barley trypsin inhibitor has been determined. The protein is a single polypeptide consisting of 121 amino acid residues and has Mr = 13,305. No free sulfhydryl groups were detected by Ellman's reagent, which indicates the presence of five disulfide bridges in the molecule. The primary site of interaction with trypsin was tentatively assigned to the arginyl-leucyl residues at positions 33 and 34. On comparison of the sequence of this inhibitor with those of other proteinase inhibitors, we found that the barley trypsin inhibitor could not be classified into any of the established families of proteinase inhibitors (Laskowski, M., Jr., and Kato, I. (1980) Annu. Rev. Biochem. 49, 593-626) and that this inhibitor should represent a new inhibitor family. On the other hand, this trypsin inhibitor showed a considerable similarity to wheat alpha-amylase inhibitor (Kashlan, N., and Richardson, M. (1981) Phytochemistry (Oxf.) 20, 1781-1784) throughout the whole sequence, suggesting a common ancestry for both proteins. This is the first case of a possible evolutionary relationship between two inhibitors directed to totally different enzymes, a proteinase and a glycosidase.

Amino Acid Sequence↗
PubMed1983

A possible evolutionary relationship between plant trypsin inhibitor, alpha-amylase inhibitor, and mammalian pancreatic secretory trypsin inhibitor (Kazal).

The amino acid sequence of the carboxyl-terminal half of barley trypsin inhibitor was found to be significantly similar to the whole sequence of bovine pancreatic secretory trypsin inhibitor (Kazal). Kazal type inhibitors and related proteins are known for the extraordinary mode of divergence among animals, and the present observation extends this to a plant for the first time. The present observation together with our previous finding of sequence homology between barley trypsin inhibitor and wheat alpha-amylase inhibitor (Odani, S., Koide, T., & Ono, T. (1982) FEBS Lett. 141, 279-282) suggest an unusual evolutionary relationship between cereal enzyme inhibitors and animal proteinase inhibitors of the Kazal type.

Amino Acid Sequence↗
PubMed1983

Three families with fast bisalbuminaemia.

We describe three cases of familial (SH, AY, and TM) fast-type bisalbuminaemia identified from 300 000 electrophoretic strips screened during the past six years. The immunological antigenicity and chemical composition of the isolated fast and normal albumins were essentially indistinguishable in all three cases. Detailed analyses on one of them (TM) by circular dichroism and fluorescent spectra measurements indicated that there was a marked change in the environment of the single tryptophan residue of the fast albumin, suggesting an alteration in the tertiary structure of the molecule. It is likely that this abnormality of the tertiary structure modulated (perturbed) the distribution of electric charges on the protein surface and thus changed its electrophoretic mobility.

Aged↗
PubMed1982

Inhibitory effect of alpha-fetoprotein on protein synthesis in a reticulocyte lysate cell-free system.

The inhibitory effect of human alpha-fetoprotein on the protein synthesis (incorporation of [3H]leucine into the total protein fraction) weas observed in a rabbit reticulocyte lysate cell-free system. The incorporation was inhibited to 50% of the control level by 14-16 microM alpha-fetoprotein, and decreased to about 15% at a concentration higher than 40 microM. An almost identical dose dependence was obtained between fetal alpha-fetoprotein and hepatoma-derived alpha-fetoprotein. This inhibitory effect on the protein synthesis was due to the interference of alpha-fetoprotein to the 40 S initiation complex formation from the ternary complex (eukaryotic initiation factor 2.GTP.Met-tRNAfMet). In contrast human serum albumin purified from fetal cord sera did not exhibit this inhibition under the same conditions. These results indicate that alpha-fetoprotein may function as a regulator of the protein synthesis in the fetal stage.

Carcinoma, Hepatocellular↗