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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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Plant Mol Biol. 1987 Jan;8(1):37-45. doi: 10.1007/BF00016432.

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

Plant molecular biology

T J Higgins, L R Beach, D Spencer, P M Chandler, P J Randall, R J Blagrove, A A Kortt, R E Guthrie

Affiliations

  1. Division of Plant Industry, CSIRO, GPO Box 1600, 2601, Canberra, A.C.T., Australia.

PMID: 24302522 DOI: 10.1007/BF00016432

Abstract

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 cDNA clone coding for one of these components has been sequenced and the deduced amino acid sequence compared with partial, chemically-determined sequences for cyanogen bromide peptides from both PA2 components. Complete amino acid sequences were obtained for the C-terminal peptides. The PA2 molecule of 230 amino acids contains four imperfect repeat sequences each of approximately 57 amino acids in length.The combined sequence data, together with a comparison of PA2-related polypeptides produced in vitro and in vivo, indicate that PA2 is synthesized without a signal sequence and does not undergo significant post-translational modification. Although both forms of PA2 contain Asn-X-Thr consensus sequences, neither form is glycosylated. Accumulation of PA2 contributes approximately 11% of the sulfur-amino acids in pea seeds (cysteine plus methionine equals 2.6 residues percent). Suppression of levels of PA2 polypeptides and their mRNAs in developing seeds of sulfur-deficient plants is less marked than that for legumin, in spite of the lower content of sulfur-amino acids in legumin.

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