@article{
 title = {Posttranslational Modifications in the Amino- Terminal Region of the Large Subunit of Ribulose- 1,5-Bisphosphate Carboxylase/Oxygenase from Several Plant Species 1},
 type = {article},
 year = {1992},
 pages = {1170-1174},
 volume = {98},
 institution = {Department of Horticulture and Landscape Architecture, Plant Physiology/Biochemistry/Molecular Biology Program, University of Kentucky, Lexington, Kentucky 40546.},
 id = {389bdd61-00e6-37de-8096-c71c11702e1b},
 created = {2011-05-20T17:26:18.000Z},
 file_attached = {false},
 profile_id = {b6c31fe8-61c6-3818-89a8-62873f3171f3},
 group_id = {7bdcaa0c-1528-351f-a09a-f8da52223946},
 last_modified = {2011-05-20T17:26:18.000Z},
 read = {false},
 starred = {false},
 authored = {false},
 confirmed = {true},
 hidden = {false},
 abstract = {A combination of limited tryptic proteolysis, reverse phasehigh performance liquid chromatography, Edman degradative sequencing, amino acid analysis, and fast-atom bombardment mass-spectrometry was used to remove and identify the first 14 to 18 N-terminal amino acid residues of the large subunit of higher plant-type ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco) from Chlamydomonas reinhardtii, Marchantia polymorpha, pea (Pisum sativum), tomato (Lycopersicon esculentum), potato (Solanum tuberosum), pepper (Capsicum annuum), soybean (Glycine max), petunia (Petunia x hybrida), cowpea (Vigna sinensis), and cucumber (Cucumis sativus) plants. The N-terminal tryptic peptide from acetylated Pro-3 to Lys-8 of the large subunit of Rubisco was identical in all species, but the amino acid sequence of the penultimate N-terminal tryptic peptide varied. Eight of the 10 species examined contained a trimethyllysyl residue at position 14 in the large subunit of Rubisco, whereas Chlamydomonas and Marchantia contained an unmodified lysyl residue at this position.},
 bibtype = {article},
 author = {Houtz, Robert L and Poneleit, Loelle and Jones, Samantha B and Royer, Malcolm and Stults, John T},
 journal = {Plant Physiology},
 number = {3}
}

{"_id":"GpdBy92BSeNAGzzn2","bibbaseid":"houtz-poneleit-jones-royer-stults-posttranslationalmodificationsintheaminoterminalregionofthelargesubunitofribulose15bisphosphatecarboxylaseoxygenasefromseveralplantspecies1-1992","downloads":0,"creationDate":"2016-03-13T16:57:31.475Z","title":"Posttranslational Modifications in the Amino- Terminal Region of the Large Subunit of Ribulose- 1,5-Bisphosphate Carboxylase/Oxygenase from Several Plant Species 1","author_short":["Houtz, R., L.","Poneleit, L.","Jones, S., B.","Royer, M.","Stults, J., T."],"year":1992,"bibtype":"article","biburl":null,"bibdata":{"title":"Posttranslational Modifications in the Amino- Terminal Region of the Large Subunit of Ribulose- 1,5-Bisphosphate Carboxylase/Oxygenase from Several Plant Species 1","type":"article","year":"1992","pages":"1170-1174","volume":"98","institution":"Department of Horticulture and Landscape Architecture, Plant Physiology/Biochemistry/Molecular Biology Program, University of Kentucky, Lexington, Kentucky 40546.","id":"389bdd61-00e6-37de-8096-c71c11702e1b","created":"2011-05-20T17:26:18.000Z","file_attached":false,"profile_id":"b6c31fe8-61c6-3818-89a8-62873f3171f3","group_id":"7bdcaa0c-1528-351f-a09a-f8da52223946","last_modified":"2011-05-20T17:26:18.000Z","read":false,"starred":false,"authored":false,"confirmed":"true","hidden":false,"abstract":"A combination of limited tryptic proteolysis, reverse phasehigh performance liquid chromatography, Edman degradative sequencing, amino acid analysis, and fast-atom bombardment mass-spectrometry was used to remove and identify the first 14 to 18 N-terminal amino acid residues of the large subunit of higher plant-type ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco) from Chlamydomonas reinhardtii, Marchantia polymorpha, pea (Pisum sativum), tomato (Lycopersicon esculentum), potato (Solanum tuberosum), pepper (Capsicum annuum), soybean (Glycine max), petunia (Petunia x hybrida), cowpea (Vigna sinensis), and cucumber (Cucumis sativus) plants. The N-terminal tryptic peptide from acetylated Pro-3 to Lys-8 of the large subunit of Rubisco was identical in all species, but the amino acid sequence of the penultimate N-terminal tryptic peptide varied. Eight of the 10 species examined contained a trimethyllysyl residue at position 14 in the large subunit of Rubisco, whereas Chlamydomonas and Marchantia contained an unmodified lysyl residue at this position.","bibtype":"article","author":"Houtz, Robert L and Poneleit, Loelle and Jones, Samantha B and Royer, Malcolm and Stults, John T","journal":"Plant Physiology","number":"3","bibtex":"@article{\n title = {Posttranslational Modifications in the Amino- Terminal Region of the Large Subunit of Ribulose- 1,5-Bisphosphate Carboxylase/Oxygenase from Several Plant Species 1},\n type = {article},\n year = {1992},\n pages = {1170-1174},\n volume = {98},\n institution = {Department of Horticulture and Landscape Architecture, Plant Physiology/Biochemistry/Molecular Biology Program, University of Kentucky, Lexington, Kentucky 40546.},\n id = {389bdd61-00e6-37de-8096-c71c11702e1b},\n created = {2011-05-20T17:26:18.000Z},\n file_attached = {false},\n profile_id = {b6c31fe8-61c6-3818-89a8-62873f3171f3},\n group_id = {7bdcaa0c-1528-351f-a09a-f8da52223946},\n last_modified = {2011-05-20T17:26:18.000Z},\n read = {false},\n starred = {false},\n authored = {false},\n confirmed = {true},\n hidden = {false},\n abstract = {A combination of limited tryptic proteolysis, reverse phasehigh performance liquid chromatography, Edman degradative sequencing, amino acid analysis, and fast-atom bombardment mass-spectrometry was used to remove and identify the first 14 to 18 N-terminal amino acid residues of the large subunit of higher plant-type ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco) from Chlamydomonas reinhardtii, Marchantia polymorpha, pea (Pisum sativum), tomato (Lycopersicon esculentum), potato (Solanum tuberosum), pepper (Capsicum annuum), soybean (Glycine max), petunia (Petunia x hybrida), cowpea (Vigna sinensis), and cucumber (Cucumis sativus) plants. The N-terminal tryptic peptide from acetylated Pro-3 to Lys-8 of the large subunit of Rubisco was identical in all species, but the amino acid sequence of the penultimate N-terminal tryptic peptide varied. Eight of the 10 species examined contained a trimethyllysyl residue at position 14 in the large subunit of Rubisco, whereas Chlamydomonas and Marchantia contained an unmodified lysyl residue at this position.},\n bibtype = {article},\n author = {Houtz, Robert L and Poneleit, Loelle and Jones, Samantha B and Royer, Malcolm and Stults, John T},\n journal = {Plant Physiology},\n number = {3}\n}","author_short":["Houtz, R., L.","Poneleit, L.","Jones, S., B.","Royer, M.","Stults, J., T."],"bibbaseid":"houtz-poneleit-jones-royer-stults-posttranslationalmodificationsintheaminoterminalregionofthelargesubunitofribulose15bisphosphatecarboxylaseoxygenasefromseveralplantspecies1-1992","role":"author","urls":{},"downloads":0,"html":""},"search_terms":["posttranslational","modifications","amino","terminal","region","large","subunit","ribulose","bisphosphate","carboxylase","oxygenase","several","plant","species","houtz","poneleit","jones","royer","stults"],"keywords":[],"authorIDs":[]}