Immunochemical Studies on <i>Arachis hypogaea</i> Proteins With Particular Reference to the Reserve Proteins. II. Protein Modification During Germination

Daussant, J.; Neucere, Navin J.; Conkerton, E. J.

doi:10.1104/pp.44.4.480

Cited by 35 publications

(14 citation statements)

References 6 publications

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“…During germination the cotyiedonary reserve proteins are broken down and the hydrolysis products are transported to the growing tissues of the seedling. During a 5-day germination at 22°C the amounts of total protein, aarachin, and aj-conarachin all decreased to about one half of the original amounts (Daussant et al 1969).…”

Section: Introductionmentioning

confidence: 84%

Activities of Various Peptidases in Cotyledons of Germinating Peanut (Arachis hypogaea)

Mikola

1976

Physiologia Plantarum

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The activities of several carboxy‐ and aminopeptidases were assayed in extracts prepared from the cotyledons of resting and germinating peanut seeds as well as from growing and fully differentiated peanut leaves. Carboxypeptidases acting on two carbobenzoxydipeptides Z‐Phe‐Ala and Z‐Ala‐Phe at pH 5.2 showed minimal activities in “resting” cotyledons, and only slight increases occurred during 7‐day germination at 28°C. In peanut leaves the corresponding activities were quite high, about 20‐ and 6‐fold compared to “germinating” cotyledons. Peptidases acting on Leu‐Tyr at pH 8.6 and on Ala‐Gly at pH 7.8 were highly active in resting cotyledons, and the activities remained essentially constant during germination; corresponding activities in leaves were much smaller (about 15–25% of those in cotyledons). “Naphthylamidases” hydrolyzing the β‐naphthylamides of Phe, Leu, and Arg at pH 7.2, were also highly active in resting cotyledons; during germination the first activity stayed at a constant level while the other two decreased progressively. Leaves showed relatively high activities on Phe‐bT‐NA and Leu‐β‐NA but only minimal activity on Arg‐β‐NA. It is tentatively concluded that the peptidases acting on Leu‐Tyr and on Ala‐Gly as well as the naphthylamidases function in the mobilization of the reserve proteins of peanut cotyledons during germination. The carboxypeptidases, in contrast, do not seem to play a major role in this process.

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Section: Introductionmentioning

confidence: 84%

Activities of Various Peptidases in Cotyledons of Germinating Peanut (Arachis hypogaea)

Mikola

1976

Physiologia Plantarum

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“…The source of this N might be the amide groups ofthe reserve proteins. The progressive acidification of the reserve proteins of the bean cotyledons (Pusztai, unpublished) appears to be a general feature of legume seed germination (Catsimpoolas, Campbell and Mayer, 1968;Daussant, Neucere and Conkerton, 1969;Shutov and Vaintraub, 1973). Thus, the general hydrolysis of the reserve proteins, located in either the protein storage organelles or in other compartments of the cells as an early event in the protein metabolism of seed germination (Amen, 1968) is open to serious doubts.…”

Section: Discussionmentioning

confidence: 99%

COMPARTMENTALIZATION IN THE COTYLEDONARY CELLS OF PHASEOLUS VULGARIS L. SEEDS: A DIFFERENTIAL SEDIMENTATION STUDY

Pusztai¹,

Croy

Grant³

et al. 1977

New Phytologist

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SUMMARYThe appearance and the yield of sedimentable organelles from the cotyledons of Phaseolus vulgaris L. were measured with respect to the influence of the method of homogenization, the choice of dry or imbibed seeds, and the composition and the concentration of the homogenization medium. Sucrose, (0.2-0.8 M), the addition of Mg^"" (2 X 10~^M) or EDTA (3 X 10~^M) or the replacement of sucrose with mannitol made little difference to the average size distribution or the amount recovered of the 21 000 ^^v ^ 10 min pelleted organelles, the main protein body-containing fraction of the homogenate. Slicing the imbibed seeds with a razor blade or by a mechanical rotary cutter combined with a short extraction was the gentlest and the most efficient method for the production of organelles. Cell homogenates were fractionated on the basis of size by differential sedimentation into several subcellular fractions. These included a residue, starch particles (300 ^ X 10 min), a main protein body fraction (21 000 ^^v X 10 min), 38 000 ^av^ 60 min pellets, 78 000 ^av X 240 min pellets and a final supernatant. The activity in these fractions of several catabolic enzymes was measured. Most of the activity of the acidic nucleases, amylases, the BAPA-ase and a substantial part of the acidic phosphatase and the cathepsin A-type enzyme(s) were found in the supernatant, while no specific DNA-ase was found in these seeds. Protein bodies contained some of the trypsin inhibitors and most (if not all) of the lectins and Glycoprotein II. Most of the endopeptidase (azoproteinase) activity of the cotyledons appeared to be tightly bound to the cell walls or to other insoluble structural elements. Protein bodies and other intracellular organelles had very little autolytic activity and, thus, the main storage proteins of the seed were not degraded during the first 4 days of germination.

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“…Deamidation of storage proteins preceding their complete proteolytic breakdown was observed in germinating seeds of several leguminous species (Daussant et al 1969, Sbtitov and Vaintraub 1973, Ganesh Kumar et al 1980. Such deamidation is particularly intensive in germinating wbeat grains (Vaintraub et al 1981).…”

Section: Introductionmentioning

confidence: 99%

Protein deamidases from germinating seeds

Vaintraub¹,

Kotova²,

Shaha³

1996

Physiol Plant

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Primed in Ueimiark -aii rigttls rsseri'ed Copyrighi © Physiotof^ia Piantaruill 1996 tSSNOnil-9317 Protein deamidases from germinatiog seeds losif Vaintraub, Ludmila Kotova and Ranajid Shaha Vaintraub, L, Kotova, L. and Shaha, R. 1996. Protein deamidases from germinating seeds. -Physiol. Planl. 96: 662-666.Enzymes catalyzing the deamidation of seed storage proteins were found in germinating seeds of kidney beans {Phaseolus vulgaris L. cv. Moldavian) and squash (Cucurbita pepo L. cv. Mozoleevskaya). They were partially purified and characterized. The properties of these enzymes closely resetnble those of the prolein deamidase in germinating wheat grains. The detection of similar protein deamidases in germinating seeds of plants belonging to phylogenetically unrelated species indicates that protein deamidases are of considerable physiological significance.

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Immunochemical Studies on Arachis hypogaea Proteins With Particular Reference to the Reserve Proteins. II. Protein Modification During Germination

Cited by 35 publications

References 6 publications

Activities of Various Peptidases in Cotyledons of Germinating Peanut (Arachis hypogaea)

Activities of Various Peptidases in Cotyledons of Germinating Peanut (Arachis hypogaea)

COMPARTMENTALIZATION IN THE COTYLEDONARY CELLS OF PHASEOLUS VULGARIS L. SEEDS: A DIFFERENTIAL SEDIMENTATION STUDY

Protein deamidases from germinating seeds

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