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cDNA and protein sequence of a major pea seed albumin (PA 2 : Mr≈26 000).

Plant molecular biology

Higgins TJ, Beach LR, Spencer D, Chandler PM, Randall PJ, Blagrove RJ, Kortt AA, Guthrie RE.
PMID: 24302522
Plant Mol Biol. 1987 Jan;8(1):37-45. doi: 10.1007/BF00016432.

Pea albumin 2 (PA2:Mr≈26000) is a major component of the albumin fraction derived from aqueous salt extracts of pea seed. Sodium dodecylsulfate-polyacrylamide gel electrophoresis and chromatography on DEAE-Sephacel resolve PA2 into two closely related components (PA2a and PA2b). A...

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Higgins TJ, Beach LR, Spencer D, et al. cDNA and protein sequence of a major pea seed albumin (PA 2 : Mr≈26 000). Plant Mol Biol. 1987;8(1):37-45doi: 10.1007/BF00016432.
Higgins, T. J., Beach, L. R., Spencer, D., Chandler, P. M., Randall, P. J., Blagrove, R. J., Kortt, A. A., & Guthrie, R. E. (1987). cDNA and protein sequence of a major pea seed albumin (PA 2 : Mr≈26 000). Plant molecular biology, 8(1), 37-45. https://doi.org/10.1007/BF00016432
Higgins, T J, et al. "cDNA and protein sequence of a major pea seed albumin (PA 2 : Mr≈26 000)." Plant molecular biology vol. 8,1 (1987): 37-45. doi: https://doi.org/10.1007/BF00016432
Higgins TJ, Beach LR, Spencer D, Chandler PM, Randall PJ, Blagrove RJ, Kortt AA, Guthrie RE. cDNA and protein sequence of a major pea seed albumin (PA 2 : Mr≈26 000). Plant Mol Biol. 1987 Jan;8(1):37-45. doi: 10.1007/BF00016432. PMID: 24302522.
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Amino Acid Sequence of Trichoanguina, a Ribosomal-Inactivating Protein from Trichosanthes anguinea Seeds.

Journal of biomedical science

Chow LP, Kamo M, Lin JY, Wang SH, Ueno Y, Tsugita A.
PMID: 11725098
J Biomed Sci. 1996 May-Jun;3(3):178-186. doi: 10.1007/BF02253098.

In this study, we sequenced a new type I ribosome-inactivating protein, trichoanguina, from the seeds of Trichosanthes anguina (snake gourd). Trichoanguina is a basic glycoprotein having an apparent molecular mass of 35.0 kD and possessing strong ribosome-inactivating activity. Trichoanguina...

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Chow LP, Kamo M, Lin JY, et al. Amino Acid Sequence of Trichoanguina, a Ribosomal-Inactivating Protein from Trichosanthes anguinea Seeds. J Biomed Sci. 1996;3(3):178-186doi: 10.1007/BF02253098.
Chow, L. P., Kamo, M., Lin, J. Y., Wang, S. H., Ueno, Y., & Tsugita, A. (1996). Amino Acid Sequence of Trichoanguina, a Ribosomal-Inactivating Protein from Trichosanthes anguinea Seeds. Journal of biomedical science, 3(3), 178-186. https://doi.org/10.1007/BF02253098
Chow, L.-P., et al. "Amino Acid Sequence of Trichoanguina, a Ribosomal-Inactivating Protein from Trichosanthes anguinea Seeds." Journal of biomedical science vol. 3,3 (1996): 178-186. doi: https://doi.org/10.1007/BF02253098
Chow LP, Kamo M, Lin JY, Wang SH, Ueno Y, Tsugita A. Amino Acid Sequence of Trichoanguina, a Ribosomal-Inactivating Protein from Trichosanthes anguinea Seeds. J Biomed Sci. 1996 May-Jun;3(3):178-186. doi: 10.1007/BF02253098. PMID: 11725098.
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A Novel Hydroxyproline-Deficient Arabinogalactan Protein Secreted by Suspension-Cultured Cells of Daucus carota (Purification and Partial Characterization).

Plant physiology

Baldwin TC, McCann MC, Roberts K.
PMID: 12231918
Plant Physiol. 1993 Sep;103(1):115-123. doi: 10.1104/pp.103.1.115.

Arabinogalactan proteins (AGPs) are secreted or membrane-associated glycoproteins that have been operationally defined as binding to [beta]-glucosyl Yariv artificial antigen, being rich in arabinose and galactose, and containing high levels of alanine, serine, and hydroxyproline. Using an anti-AGP monoclonal...

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Baldwin TC, McCann MC, Roberts K. A Novel Hydroxyproline-Deficient Arabinogalactan Protein Secreted by Suspension-Cultured Cells of Daucus carota (Purification and Partial Characterization). Plant Physiol. 1993;103(1):115-123doi: 10.1104/pp.103.1.115.
Baldwin, T. C., McCann, M. C., & Roberts, K. (1993). A Novel Hydroxyproline-Deficient Arabinogalactan Protein Secreted by Suspension-Cultured Cells of Daucus carota (Purification and Partial Characterization). Plant physiology, 103(1), 115-123. https://doi.org/10.1104/pp.103.1.115
Baldwin, T. C., et al. "A Novel Hydroxyproline-Deficient Arabinogalactan Protein Secreted by Suspension-Cultured Cells of Daucus carota (Purification and Partial Characterization)." Plant physiology vol. 103,1 (1993): 115-123. doi: https://doi.org/10.1104/pp.103.1.115
Baldwin TC, McCann MC, Roberts K. A Novel Hydroxyproline-Deficient Arabinogalactan Protein Secreted by Suspension-Cultured Cells of Daucus carota (Purification and Partial Characterization). Plant Physiol. 1993 Sep;103(1):115-123. doi: 10.1104/pp.103.1.115. PMID: 12231918; PMCID: PMC158953.
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Parallel solid-phase synthesis of trisubstituted triazinobenzimidazolediones.

Journal of combinatorial chemistry

Klein G, Acharya AN, Ostresh JM, Houghten RA.
PMID: 12099852
J Comb Chem. 2002 Jul-Aug;4(4):345-51. doi: 10.1021/cc010089k.

An efficient method for the solid-phase synthesis of trisubstituted [1,3,5]triazino[1,2-a]benzimidazole-2,4(3H,10H)-diones from resin-bound amino acids is described. N-acylation of the primary amine of a resin-bound amino acid with 4-fluoro-3-nitrobenzoic acid, followed by displacement of the fluoro group and reduction of...

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Klein G, Acharya AN, Ostresh JM, et al. Parallel solid-phase synthesis of trisubstituted triazinobenzimidazolediones. J Comb Chem. 2002;4(4):345-51doi: 10.1021/cc010089k.
Klein, G., Acharya, A. N., Ostresh, J. M., & Houghten, R. A. (2002). Parallel solid-phase synthesis of trisubstituted triazinobenzimidazolediones. Journal of combinatorial chemistry, 4(4), 345-51. https://doi.org/10.1021/cc010089k
Klein, Gérard, et al. "Parallel solid-phase synthesis of trisubstituted triazinobenzimidazolediones." Journal of combinatorial chemistry vol. 4,4 (2002): 345-51. doi: https://doi.org/10.1021/cc010089k
Klein G, Acharya AN, Ostresh JM, Houghten RA. Parallel solid-phase synthesis of trisubstituted triazinobenzimidazolediones. J Comb Chem. 2002 Jul-Aug;4(4):345-51. doi: 10.1021/cc010089k. PMID: 12099852.
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Isolation and characterization of the cyanogen bromide peptides from the alpha2 chain of calf skin collagen.

FEBS letters

Fietzek PP, Münch M, Breitkreutz D, Kühn K.
PMID: 11947677
FEBS Lett. 1970 Aug 17;9(4):229-231. doi: 10.1016/0014-5793(70)80362-3.

No abstract available.

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Fietzek PP, Münch M, Breitkreutz D, et al. Isolation and characterization of the cyanogen bromide peptides from the alpha2 chain of calf skin collagen. FEBS Lett. 1970;9(4):229-231doi: 10.1016/0014-5793(70)80362-3.
Fietzek, P. P., Münch, M., Breitkreutz, D., & Kühn, K. (1970). Isolation and characterization of the cyanogen bromide peptides from the alpha2 chain of calf skin collagen. FEBS letters, 9(4), 229-231. https://doi.org/10.1016/0014-5793(70)80362-3
Fietzek, P P., et al. "Isolation and characterization of the cyanogen bromide peptides from the alpha2 chain of calf skin collagen." FEBS letters vol. 9,4 (1970): 229-231. doi: https://doi.org/10.1016/0014-5793(70)80362-3
Fietzek PP, Münch M, Breitkreutz D, Kühn K. Isolation and characterization of the cyanogen bromide peptides from the alpha2 chain of calf skin collagen. FEBS Lett. 1970 Aug 17;9(4):229-231. doi: 10.1016/0014-5793(70)80362-3. PMID: 11947677.
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Binding Specificity and Possible Analytical Applications of the Cytokinin-binding Antibody, Anti-N-Benzyladenosine.

Plant physiology

Constantinidou HA.
PMID: 16660648
Plant Physiol. 1978 Dec;62(6):968-74. doi: 10.1104/pp.62.6.968.

Antibodies elicited in rabbits by immunization with an N(6)-benzyladenosine-bovine serum albumin conjugate bound N(6)-benzyladenosine specifically. The affinity constants and specific binding site concentrations for a number of cytokinins and related compounds were estimated by nonlinear least squares analysis of...

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Constantinidou HA. Binding Specificity and Possible Analytical Applications of the Cytokinin-binding Antibody, Anti-N-Benzyladenosine. Plant Physiol. 1978;62(6):968-74doi: 10.1104/pp.62.6.968.
Constantinidou, H. A. (1978). Binding Specificity and Possible Analytical Applications of the Cytokinin-binding Antibody, Anti-N-Benzyladenosine. Plant physiology, 62(6), 968-74. https://doi.org/10.1104/pp.62.6.968
Constantinidou, H A. "Binding Specificity and Possible Analytical Applications of the Cytokinin-binding Antibody, Anti-N-Benzyladenosine." Plant physiology vol. 62,6 (1978): 968-74. doi: https://doi.org/10.1104/pp.62.6.968
Constantinidou HA. Binding Specificity and Possible Analytical Applications of the Cytokinin-binding Antibody, Anti-N-Benzyladenosine. Plant Physiol. 1978 Dec;62(6):968-74. doi: 10.1104/pp.62.6.968. PMID: 16660648; PMCID: PMC1092264.
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P(700) Chlorophyll a-Protein : Purification, Characterization, and Antibody Preparation.

Plant physiology

Vierling E, Alberte RS.
PMID: 16663057
Plant Physiol. 1983 Jul;72(3):625-33. doi: 10.1104/pp.72.3.625.

The P(700) chlorophyll alpha-protein was purified by preparative sodium dodecyl sulfate (SDS) gel electrophoresis from SDS-solubilized barley (Hordeum vulgare L., cv Himalaya) chloroplast membranes. After elution from the gel in the presence of 0.05 to 0.1% Triton X-100, the...

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Vierling E, Alberte RS. P(700) Chlorophyll a-Protein : Purification, Characterization, and Antibody Preparation. Plant Physiol. 1983;72(3):625-33doi: 10.1104/pp.72.3.625.
Vierling, E., & Alberte, R. S. (1983). P(700) Chlorophyll a-Protein : Purification, Characterization, and Antibody Preparation. Plant physiology, 72(3), 625-33. https://doi.org/10.1104/pp.72.3.625
Vierling, E, and Alberte, R S. "P(700) Chlorophyll a-Protein : Purification, Characterization, and Antibody Preparation." Plant physiology vol. 72,3 (1983): 625-33. doi: https://doi.org/10.1104/pp.72.3.625
Vierling E, Alberte RS. P(700) Chlorophyll a-Protein : Purification, Characterization, and Antibody Preparation. Plant Physiol. 1983 Jul;72(3):625-33. doi: 10.1104/pp.72.3.625. PMID: 16663057; PMCID: PMC1066292.
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l-Arginine and l-Canavanine Metabolism in Jack Bean, Canavalia ensiformis (L.) DC. and Soybean, Glycine max (L.) Merr.

Plant physiology

Downum KR, Rosenthal GA, Cohen WS.
PMID: 16663352
Plant Physiol. 1983 Dec;73(4):965-8. doi: 10.1104/pp.73.4.965.

Studies have been conducted with the arginase (l-arginine amidinohydrolase, EC 3.5.3.1) of two legumes: jack bean, Canavalia ensiformis (L.) DC., a l-canavanine-containing plant and soybean, Glycine max, a canavanine-free species. Analyses of the arginase obtained from gradient-purified mitochondria of...

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Downum KR, Rosenthal GA, Cohen WS. l-Arginine and l-Canavanine Metabolism in Jack Bean, Canavalia ensiformis (L.) DC. and Soybean, Glycine max (L.) Merr. Plant Physiol. 1983;73(4):965-8doi: 10.1104/pp.73.4.965.
Downum, K. R., Rosenthal, G. A., & Cohen, W. S. (1983). l-Arginine and l-Canavanine Metabolism in Jack Bean, Canavalia ensiformis (L.) DC. and Soybean, Glycine max (L.) Merr. Plant physiology, 73(4), 965-8. https://doi.org/10.1104/pp.73.4.965
Downum, K R, et al. "l-Arginine and l-Canavanine Metabolism in Jack Bean, Canavalia ensiformis (L.) DC. and Soybean, Glycine max (L.) Merr." Plant physiology vol. 73,4 (1983): 965-8. doi: https://doi.org/10.1104/pp.73.4.965
Downum KR, Rosenthal GA, Cohen WS. l-Arginine and l-Canavanine Metabolism in Jack Bean, Canavalia ensiformis (L.) DC. and Soybean, Glycine max (L.) Merr. Plant Physiol. 1983 Dec;73(4):965-8. doi: 10.1104/pp.73.4.965. PMID: 16663352; PMCID: PMC1066589.
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Stability of nicotinamide adenine dinucleotide immobilized to cyanogen bromide activated agarose.

Biotechnology and bioengineering

Schall CA, Wiencek JM.
PMID: 18629958
Biotechnol Bioeng. 1997 Jan 05;53(1):41-8. doi: 10.1002/(SICI)1097-0290(19970105)53:1<41::AID-BIT7>3.0.CO;2-Z.

The stability of NAD(H) immobilized to a crosslinked agarose support (Sepharose(R)-4B) was examined in buffer solutions at a pH of 7.0 and 8.5. Specifically, this study investigated particle attrition and ligand leakage rates from a cyanogen bromide activated agarose...

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Schall CA, Wiencek JM. Stability of nicotinamide adenine dinucleotide immobilized to cyanogen bromide activated agarose. Biotechnol Bioeng. 1997;53(1):41-8doi: 10.1002/(SICI)1097-0290(19970105)53:1<41::AID-BIT7>3.0.CO;2-Z.
Schall, C. A., & Wiencek, J. M. (1997). Stability of nicotinamide adenine dinucleotide immobilized to cyanogen bromide activated agarose. Biotechnology and bioengineering, 53(1), 41-8. https://doi.org/10.1002/(SICI)1097-0290(19970105)53:1<41::AID-BIT7>3.0.CO;2-Z
Schall, C A, and Wiencek, J M. "Stability of nicotinamide adenine dinucleotide immobilized to cyanogen bromide activated agarose." Biotechnology and bioengineering vol. 53,1 (1997): 41-8. doi: https://doi.org/10.1002/(SICI)1097-0290(19970105)53:1<41::AID-BIT7>3.0.CO;2-Z
Schall CA, Wiencek JM. Stability of nicotinamide adenine dinucleotide immobilized to cyanogen bromide activated agarose. Biotechnol Bioeng. 1997 Jan 05;53(1):41-8. doi: 10.1002/(SICI)1097-0290(19970105)53:1<41::AID-BIT7>3.0.CO;2-Z. PMID: 18629958.
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The C-terminal sequences of the heavy chains of human immunoglobulin G myeloma proteins of differing isotopes and allotypes.

The Biochemical journal

Prahl JW.
PMID: 16742526
Biochem J. 1967 Dec;105(3):1019-28. doi: 10.1042/bj1051019.

The sequences of the C-terminal octadecapeptides obtained by cyanogen bromide cleavage of the gamma-chains of myeloma proteins of the four subclasses, and a urinary heavy-chain-disease protein, have been determined. Although the sequences were markedly homologous, unique replacements were identified...

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Prahl JW. The C-terminal sequences of the heavy chains of human immunoglobulin G myeloma proteins of differing isotopes and allotypes. Biochem J. 1967;105(3):1019-28doi: 10.1042/bj1051019.
Prahl, J. W. (1967). The C-terminal sequences of the heavy chains of human immunoglobulin G myeloma proteins of differing isotopes and allotypes. The Biochemical journal, 105(3), 1019-28. https://doi.org/10.1042/bj1051019
Prahl, J W. "The C-terminal sequences of the heavy chains of human immunoglobulin G myeloma proteins of differing isotopes and allotypes." The Biochemical journal vol. 105,3 (1967): 1019-28. doi: https://doi.org/10.1042/bj1051019
Prahl JW. The C-terminal sequences of the heavy chains of human immunoglobulin G myeloma proteins of differing isotopes and allotypes. Biochem J. 1967 Dec;105(3):1019-28. doi: 10.1042/bj1051019. PMID: 16742526; PMCID: PMC1198421.
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Synthesis and processing of maize storage proteins in Xenopus laevis oocytes.

Proceedings of the National Academy of Sciences of the United States of America

Larkins BA, Pedersen K, Handa AK, Hurkman WJ, Smith LD.
PMID: 16592743
Proc Natl Acad Sci U S A. 1979 Dec;76(12):6448-52. doi: 10.1073/pnas.76.12.6448.

Xenopus oocytes injected with zein mRNAs efficiently synthesized maize storage proteins for prolonged periods. Under optimal conditions, zein was synthesized at 3 ng/hr and represented approximately 10% of the total protein synthesized in the oocyte. The mRNA from the...

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Larkins BA, Pedersen K, Handa AK, et al. Synthesis and processing of maize storage proteins in Xenopus laevis oocytes. Proc Natl Acad Sci U S A. 1979;76(12):6448-52doi: 10.1073/pnas.76.12.6448.
Larkins, B. A., Pedersen, K., Handa, A. K., Hurkman, W. J., & Smith, L. D. (1979). Synthesis and processing of maize storage proteins in Xenopus laevis oocytes. Proceedings of the National Academy of Sciences of the United States of America, 76(12), 6448-52. https://doi.org/10.1073/pnas.76.12.6448
Larkins, B A, et al. "Synthesis and processing of maize storage proteins in Xenopus laevis oocytes." Proceedings of the National Academy of Sciences of the United States of America vol. 76,12 (1979): 6448-52. doi: https://doi.org/10.1073/pnas.76.12.6448
Larkins BA, Pedersen K, Handa AK, Hurkman WJ, Smith LD. Synthesis and processing of maize storage proteins in Xenopus laevis oocytes. Proc Natl Acad Sci U S A. 1979 Dec;76(12):6448-52. doi: 10.1073/pnas.76.12.6448. PMID: 16592743; PMCID: PMC411882.
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Primary structure of goat myoglobin.

Meat science

Suman SP, Joseph P, Li S, Steinke L, Fontaine M.
PMID: 20416681
Meat Sci. 2009 Aug;82(4):456-60. doi: 10.1016/j.meatsci.2009.02.017. Epub 2009 Mar 10.

Color stability attributes of goat meat are different from those of sheep meat, possibly due to species-specific differences in myoglobin (Mb) biochemistry. An examination of post-genomic era protein databases revealed that the primary structure of goat Mb has not...

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Suman SP, Joseph P, Li S, et al. Primary structure of goat myoglobin. Meat Sci. 2009;82(4):456-60doi: 10.1016/j.meatsci.2009.02.017.
Suman, S. P., Joseph, P., Li, S., Steinke, L., & Fontaine, M. (2009). Primary structure of goat myoglobin. Meat science, 82(4), 456-60. https://doi.org/10.1016/j.meatsci.2009.02.017
Suman, S P, et al. "Primary structure of goat myoglobin." Meat science vol. 82,4 (2009): 456-60. doi: https://doi.org/10.1016/j.meatsci.2009.02.017
Suman SP, Joseph P, Li S, Steinke L, Fontaine M. Primary structure of goat myoglobin. Meat Sci. 2009 Aug;82(4):456-60. doi: 10.1016/j.meatsci.2009.02.017. Epub 2009 Mar 10. PMID: 20416681.
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Showing 1 to 12 of 102 entries