NCIMB 9290
NCIMB 9290
规格:
货期:
编号:TS389159
品牌:Testobio
| NCIMB number | NCIMB 9290 |
| Deposit type | Bacteria |
| Type strain | Yes |
| GMO | No |
| Taxon name | Pedobacter heparinus |
| Preservation method | Lyophilised |
| Preserved as | Cytophaga heparina |
| Price band | A |
| Media | 001 |
| Gas regime | aerobic |
| Growth factors (and/or information) | NA, 25C, 3d: moderate growth, soft consistency |
| ACDP category | 1 |
| Colony Edge | Entire |
| Colony Surface | Smooth |
| Colony Shape | Circular |
| Colony Elevation | Raised |
| Colony Colour | Yellowish |
| Colony Opacity | Translucent/Transp. |
| Cellular Shape | Rod |
| Cellular Size | fairly short |
| Cellular Motility | Glider |
| Gram stain | Gram Negative |
| Cellular (Other) | Straight Or Slightly Curved Axis, Parallel Sides, Rounded Ends |
| Depositor Company | American Type Culture Collection (ATCC) |
| Depositor Address | 12301 Parklawn Drive Rockville Maryland 20852 U.S.A. |
| Source | Dry soil |
| Date of Accession | 25/02/1971 |
| History | E.D.Korn |
| Other collection IDs | ATCC13125 DSM2366 IAM12655 IFO12017 |
| Yeast? | False |
| K12 | No |
| References | Payza A.N. and Korn E.D. (1956) Nature, London 177 p88 Payza A.N. and Korn E.D. (1956) J. biol. Chem. 223 p853 Korn E.D., Payza A.N. (1956) J. biol. Chem. 223 p859 Korn E.D. (1957) J. biol. Chem. 226 p827 Korn E.D. (1957) J. biol. Chem. 226 p841 Linker A. et al (1960) J. biol. Chem. 235 p3061 Mitchell T.G., Hendrie M.S. and Shewan J.M. (1969) J. appl. Bact. 32 pp40-50 Karapally J.C. and Dietrich C.P. (1970) Can. J. Biochem. 48(2) p164. Suzuki S. (1972) Meth. Enzym. 28B pp911-917. Chondroitinases from Proteus vulgaris and Flavobacterium heparinum. Linker A. and Hovingh P. (1972) Meth. Enzym. 28B pp902-911. Heparinase and heparitinase from Flavobacteria. Perry L.B. (1973) J. appl. Bact. 36 p227 Dietrich C.P., Silva M.E. and Michelacci Y.M. (1973) J. biol. Chem. 248 p6408. Sequential degradation of heparin in Flavobacterium heparinum. Purification and properties of five enzymes involved in heparin degradation. Silva M.E. and Dietrich C.P. (1973) Biochimie 55 p1101. Studies on the induction of heparin degrading enzymes in Flavobacterium heparinum. II. Structural requirements of the inducer. Embery G. and Day J. M. (1973) Biochem. Soc. Trans. 1 pp271-274. An alternative pathway for enzymic degradation of 35S heparin by Flavobacterium heparinum Silva M.E. and Dietrich C.P. (1974) Biochem. biophys. Res. Comm. 56 p965. Isolation and partial characterization of three induced enzymes from F. heparinum involved in the degradation of heparin and heparitin sulfates. Michelacci Y.M. and Dietrich C.P. (1974) Biochem. biophys. Res. Comm. 56 p973. Isolation and partial characterization of an induced chondroitinase B from F. heparinum. Int. J. syst. Bact. (1993) 43 p864 IJSB 48:175 The tmRNA website: reductive evolution of tmRNA in plastids and other endosymbionts, Nucleic Acids Res 32(Databaseissue), D104-D108, 2004 (Unknown), Int J Syst Bacteriol 48, 629, 1998 (Unknown), J Biol Chem 233, 853, 1956 Validation of the publication of new names and new combinations previously effectively published outside the IJSB. List No. 47, Int J Syst Bacteriol 43, 864-865, 1993 Approved Lists of Bacterial Names, Int J Syst Bacteriol 30, 225-420, 1980 Chemotaxonomic and phenotypic characterization of the strains of species in the Flavobacterium-Cytophaga complex, J Gen Appl Microbiol 27, 57-107, 1981 Proposals of Sphingobacterium faecium sp. nov., Sphingobacterium piscium sp. nov., Sphingobacterium heparinum comb. nov., Sphingobacterium thalpophilum comb. nov. and two genospecies of the genus Sphingobacterium and synonymy of Flavobacterium yabuuchiae and Sphingobacterium spiritivorum, J Gen Appl Microbiol 38, 465-482, 1992 5S rRNA sequences of representatives of the genera Chlorobium, Prosthecochloris, Thermomicrobium, Cytophaga, Flavobacterium, Flexibacter and Saprospira and a discussion of the evolution of eubacteria in general, J Gen Microbiol 136(1), 11-18, 1990 Deoxyribonucleic acid relatedness of some menaquinone-producing Flavobacterium and Cytophaga strains, Antonie Van Leeuwenhoek 46(1), 41-49, 1980 Phylogenetic analysis of genus Marinilabilia and related bacteria based on the amino acid sequences of gyrB and emended description of Marinilabilia salmonicolor with Marinilabilia agarovorans as its subjective synonym, Int J Syst Bacteriol 49 Pt 4, 1551-1557, 1999 Bacterial degradation of heparin, Nature 177(4498), 88-89, 1956 Chondroitinases from Proteus vulgaris and Flavobacterium heparinum, Methods Enzymol XXVIII B, 911-917, 1972 Classification of heparinolytic bacteria into a new genus, Pedobacter, comprising four species: Pedobacter heparinus comb. nov., Pedobacter piscium comb. nov., Pedobacter africanus sp. nov. and Pedobacter saltans sp. nov. proposal of the family Sphingobacteriaceae fam. nov, Int J Syst Bacteriol 48 Pt 1, 165-177, 1998 Complete genome sequence of Pedobacter heparinus type strain (HIM 762-3), Stand Genomic Sci 1(1), 54-62, 2009 Description and taxonomic status of Cytophaga heparina (Payza and Korn) comb. nov. (Basonym: Flavobacterium heparinum Payza and Korn 1956), Int J Syst Bacteriol 30, 473-475, 1980 Enzymic degradation of heparin. A sulphamidase and a sulphoesterase from Flavobacterium heparinum, Biochem J 111(1), 91-95, 1969 Heparinase and heparinitase from flavobacteria, Methods Enzymol XXVIII B, 902-911, 1972 Heparinase production by Flavobacterium heparinum, Appl Environ Microbiol 41, 360-365, 1981 McDuffie, N. M. (ed.). Heparin: structure, cellular functions and clinical applications. Academic Press, New York 1979, (journal unknown) , 3-24, 1979 Pedobacter cryoconitis sp. nov., a facultative psychrophile from alpine glacier cryoconite, Int J Syst Evol Microbiol 53(5), 1291-1296, 2003 Purification of an unusual alpha-glucuronidase from flavobacteria, Biochemistry 11, 568-572, 1972 Sequential degradation of heparin in Flavobacterium heparinum: purification and properties of five enzymes involved in heparin degradation, J Biol Chem 248, 6408-6415, 1973 The degradation of heparin by bacterial enzymes. I. Adaptation and lyophilized cells, J Biol Chem 223(2), 853-858, 1956 |
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| NCIMB number | NCIMB 9290 |
| Deposit type | Bacteria |
| Type strain | Yes |
| GMO | No |
| Taxon name | Pedobacter heparinus |
| Preservation method | Lyophilised |
| Preserved as | Cytophaga heparina |
| Price band | A |
| Media | 001 |
| Gas regime | aerobic |
| Growth factors (and/or information) | NA, 25C, 3d: moderate growth, soft consistency |
| ACDP category | 1 |
| Colony Edge | Entire |
| Colony Surface | Smooth |
| Colony Shape | Circular |
| Colony Elevation | Raised |
| Colony Colour | Yellowish |
| Colony Opacity | Translucent/Transp. |
| Cellular Shape | Rod |
| Cellular Size | fairly short |
| Cellular Motility | Glider |
| Gram stain | Gram Negative |
| Cellular (Other) | Straight Or Slightly Curved Axis, Parallel Sides, Rounded Ends |
| Depositor Company | American Type Culture Collection (ATCC) |
| Depositor Address | 12301 Parklawn Drive Rockville Maryland 20852 U.S.A. |
| Source | Dry soil |
| Date of Accession | 25/02/1971 |
| History | E.D.Korn |
| Other collection IDs | ATCC13125 DSM2366 IAM12655 IFO12017 |
| Yeast? | False |
| K12 | No |
| References | Payza A.N. and Korn E.D. (1956) Nature, London 177 p88 Payza A.N. and Korn E.D. (1956) J. biol. Chem. 223 p853 Korn E.D., Payza A.N. (1956) J. biol. Chem. 223 p859 Korn E.D. (1957) J. biol. Chem. 226 p827 Korn E.D. (1957) J. biol. Chem. 226 p841 Linker A. et al (1960) J. biol. Chem. 235 p3061 Mitchell T.G., Hendrie M.S. and Shewan J.M. (1969) J. appl. Bact. 32 pp40-50 Karapally J.C. and Dietrich C.P. (1970) Can. J. Biochem. 48(2) p164. Suzuki S. (1972) Meth. Enzym. 28B pp911-917. Chondroitinases from Proteus vulgaris and Flavobacterium heparinum. Linker A. and Hovingh P. (1972) Meth. Enzym. 28B pp902-911. Heparinase and heparitinase from Flavobacteria. Perry L.B. (1973) J. appl. Bact. 36 p227 Dietrich C.P., Silva M.E. and Michelacci Y.M. (1973) J. biol. Chem. 248 p6408. Sequential degradation of heparin in Flavobacterium heparinum. Purification and properties of five enzymes involved in heparin degradation. Silva M.E. and Dietrich C.P. (1973) Biochimie 55 p1101. Studies on the induction of heparin degrading enzymes in Flavobacterium heparinum. II. Structural requirements of the inducer. Embery G. and Day J. M. (1973) Biochem. Soc. Trans. 1 pp271-274. An alternative pathway for enzymic degradation of 35S heparin by Flavobacterium heparinum Silva M.E. and Dietrich C.P. (1974) Biochem. biophys. Res. Comm. 56 p965. Isolation and partial characterization of three induced enzymes from F. heparinum involved in the degradation of heparin and heparitin sulfates. Michelacci Y.M. and Dietrich C.P. (1974) Biochem. biophys. Res. Comm. 56 p973. Isolation and partial characterization of an induced chondroitinase B from F. heparinum. Int. J. syst. Bact. (1993) 43 p864 IJSB 48:175 The tmRNA website: reductive evolution of tmRNA in plastids and other endosymbionts, Nucleic Acids Res 32(Databaseissue), D104-D108, 2004 (Unknown), Int J Syst Bacteriol 48, 629, 1998 (Unknown), J Biol Chem 233, 853, 1956 Validation of the publication of new names and new combinations previously effectively published outside the IJSB. List No. 47, Int J Syst Bacteriol 43, 864-865, 1993 Approved Lists of Bacterial Names, Int J Syst Bacteriol 30, 225-420, 1980 Chemotaxonomic and phenotypic characterization of the strains of species in the Flavobacterium-Cytophaga complex, J Gen Appl Microbiol 27, 57-107, 1981 Proposals of Sphingobacterium faecium sp. nov., Sphingobacterium piscium sp. nov., Sphingobacterium heparinum comb. nov., Sphingobacterium thalpophilum comb. nov. and two genospecies of the genus Sphingobacterium and synonymy of Flavobacterium yabuuchiae and Sphingobacterium spiritivorum, J Gen Appl Microbiol 38, 465-482, 1992 5S rRNA sequences of representatives of the genera Chlorobium, Prosthecochloris, Thermomicrobium, Cytophaga, Flavobacterium, Flexibacter and Saprospira and a discussion of the evolution of eubacteria in general, J Gen Microbiol 136(1), 11-18, 1990 Deoxyribonucleic acid relatedness of some menaquinone-producing Flavobacterium and Cytophaga strains, Antonie Van Leeuwenhoek 46(1), 41-49, 1980 Phylogenetic analysis of genus Marinilabilia and related bacteria based on the amino acid sequences of gyrB and emended description of Marinilabilia salmonicolor with Marinilabilia agarovorans as its subjective synonym, Int J Syst Bacteriol 49 Pt 4, 1551-1557, 1999 Bacterial degradation of heparin, Nature 177(4498), 88-89, 1956 Chondroitinases from Proteus vulgaris and Flavobacterium heparinum, Methods Enzymol XXVIII B, 911-917, 1972 Classification of heparinolytic bacteria into a new genus, Pedobacter, comprising four species: Pedobacter heparinus comb. nov., Pedobacter piscium comb. nov., Pedobacter africanus sp. nov. and Pedobacter saltans sp. nov. proposal of the family Sphingobacteriaceae fam. nov, Int J Syst Bacteriol 48 Pt 1, 165-177, 1998 Complete genome sequence of Pedobacter heparinus type strain (HIM 762-3), Stand Genomic Sci 1(1), 54-62, 2009 Description and taxonomic status of Cytophaga heparina (Payza and Korn) comb. nov. (Basonym: Flavobacterium heparinum Payza and Korn 1956), Int J Syst Bacteriol 30, 473-475, 1980 Enzymic degradation of heparin. A sulphamidase and a sulphoesterase from Flavobacterium heparinum, Biochem J 111(1), 91-95, 1969 Heparinase and heparinitase from flavobacteria, Methods Enzymol XXVIII B, 902-911, 1972 Heparinase production by Flavobacterium heparinum, Appl Environ Microbiol 41, 360-365, 1981 McDuffie, N. M. (ed.). Heparin: structure, cellular functions and clinical applications. Academic Press, New York 1979, (journal unknown) , 3-24, 1979 Pedobacter cryoconitis sp. nov., a facultative psychrophile from alpine glacier cryoconite, Int J Syst Evol Microbiol 53(5), 1291-1296, 2003 Purification of an unusual alpha-glucuronidase from flavobacteria, Biochemistry 11, 568-572, 1972 Sequential degradation of heparin in Flavobacterium heparinum: purification and properties of five enzymes involved in heparin degradation, J Biol Chem 248, 6408-6415, 1973 The degradation of heparin by bacterial enzymes. I. Adaptation and lyophilized cells, J Biol Chem 223(2), 853-858, 1956 |
