A Study of Protein Bodies During Germination of Peanut (Arachis Hypogaea) Seed

Bagley, Bill W.; Cherry, Joe H.; Rollins, Mary L.; Altschul, Aaron M.

doi:10.2307/2440027

Cited by 55 publications

(31 citation statements)

References 6 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…With increased incubation times, this result was usually masked by complete dissolution of the gelatin between the vascular bundles (as in Fig. 1, F, G, and H) (20), where mobilization starts at the periphery, but is similar to that in Phaseolus vulgaris (15) and Arachis hypogaea (1).…”

Section: Harris and Chrispeelsmentioning

confidence: 94%

See 1 more Smart Citation

Histochemical and Biochemical Observations on Storage Protein Metabolism and Protein Body Autolysis in Cotyledons of Germinating Mung Beans

1975

View full text Add to dashboard Cite

Storage protein hydrolysis in the cotyledons of germinating mung beans (Phaseolus aureus Roxb.) was examined by histochemical techniques, and the autolytic capacity of isolated protein bodies was studied with biochemical methods. The localization of endopeptidase activity within the cotyledons was studied using an India ink-gelatin film technique. After 24 hours of imbibition, a low level of endopeptidase activity was found throughout the storage tissues of the cotyledons. A marked increase in activity was noted in cells farthest from the vascular bundles 48 to 60 hours after the start of imbibition. The decrease in storage protein followed the same spatial distribution starting in the cells farthest from the bundles. The cotyledons contain a population of cells in various stages of endopeptidase activity enhancement and storage protein degradation. A wave of endopeptidase activity moves progressively through the cotyledons towards the vascular bundles leaving behind areas devoid of stored reserves and low in endopeptidase activity. Observations on the morphology of protein bodies during germination indicate that the membrane surrounding them remains intact, while the reserves disappear. This result suggests that the protein bodies may be undergoing autolysis. To determine whether this may indeed be the case, protein bodies were isolated from the meal of mung bean seeds using an aqueous medium containing 80% glycerol. The protein body preparations and the cytoplasm were assayed for the presence of a number of enzymes which may be involved in the breakdown of the storage proteins. The protein bodies contained all, or nearly all, of the carboxypeptidase, a-mannosidase, N-acetyl-,8-glucosaminidase, and

show abstract

Section: Harris and Chrispeelsmentioning

confidence: 94%

“…Germination of these seeds is often accompanied by the swelling of the protein bodies (1,4,15). This swelling is probably the result of protein hydrolysis leading to an increase in osmotic pressure which in turn causes the protein bodies to take up more water.…”

mentioning

confidence: 99%

Histochemical and Biochemical Observations on Storage Protein Metabolism and Protein Body Autolysis in Cotyledons of Germinating Mung Beans

1975

View full text Add to dashboard Cite

show abstract

“…The tissues were either postfixed (see below) or allowed to warm to room temperature in the last buffer rinse and then incubated in one of the media listed below. These procedures are variations of several histochemical methods (8,11,23) (2,7,14,16). Both are utilized by the embryonic axis during germination and are largely gone by the 6th day of germination ( Fig.…”

mentioning

confidence: 99%

Studies on Seeds

Mollenhauer

Totten

1970

Plant Physiol.

View full text Add to dashboard Cite

Glyoxysomes, a form of microbody, are present in castor bean endosperm during the first 8 days of seed germination.They have a "typical" microbody form and are shown histochemically to contain catalase. The catalase label is distributed throughout the microbody and is not an exclusive feature of the crystalline or amorphous core.Castor bean endosperm contain a second cytosome, only slightly larger than the glyoxysomes, which is bound by a rough-surfaced membrane and which does not label for catalase. We have not observed these cytosomes in other tissues, suggesting that they may have a specific cellular function characteristic of castor bean endosperm.Glyoxysomes are a morphologically and biochemically unique component of many cells (3,4,12,13). They are a form of microbody containing enzymes of the glyoxylate cycle. Like peroxisomes and other types of microbodies, they also contain catalase and glycolic acid oxidase (4).Microbodies are present in castor bean endosperm throughout seed development, dormancy, and germination, but enzymes of the glyoxylate cycle do not reach maximal activity until the 4th or 5th day of seed germination (5, 12). There is no indication from ultrastructural studies that microbodies disappear, reform, or change significantly in number, in relation to the appearance of enzymes of the glyoxylate cycle. It is assumed, therefore, that glyoxysomes are somehow evolved from microbodies by enzyme activation or by gradual replacement of existing microbodies with those of the glyoxysome type.We have isolated microbodies, as well as glyoxysomes, from a number of seeds and have found that the glyoxysome fractions from castor bean endosperm sometimes contain a contaminating particle that is similar in size to glyoxysomes. Studies in vivo of germinating castor bean confirm that a microbody-like particle does exist in the endosperm and is most easily recognized when enzymes of the glyoxylate cycle are active. We thought initially that these new particles might be related, or equivalent, to glyoxysomes and, therefore, initiated these studies. This report describes these new particles and compares them structurally and histochemically with microbodies. 2"Studies on Seeds, I through IV" will appear in the Journal of Cell Biology. MATERIALS AND METHODSCastor bean (Hale variety and Baker variety 296 obtained from The Baker Castor Oil Co., La Mesa, Calif.) seeds were scarified and the seeds were soaked in water for 2 to 24 hr. The seeds were germinated for 3 to 8 days in the dark at 28 C in vermiculite moistened with distilled water.Slices of endosperm were prefixed in a mixture of 2% glutaraldehyde-2 % paraformaldehyde in 0.05 M collidine buffer containing 0.06 M sucrose, pH 7.3 to 7.4 for 2 hr, cold. After prefixation, the tissues were rinsed in six 5-to 10-min changes of buffer. Unless otherwise indicated, the buffer used was 0.05 M collidine with 0.06 M sucrose, pH 7.3 to 7.4. The tissues were either postfixed (see below) or allowed to warm to room temperature in the last buffer rinse and then ...

show abstract

“…Then, eventually the bodies became irregularly shaped and sometimes appeared to be coalesced into a large single mass. These observations of protein bodies are similar to those reported for other tissues, such as peanut (Bagley et al, 1963), pea (Bain and Mercer, 1966), Yucca (Horner and Amott, 1965) and Phaseolus (Opik, 1966). Suryanarayana (1976), suggests that protein bodies in soybean cotyledons undergo progressive fragmentation into smaller particles and finally disappear from most cotyledon cells by 9 days after germination.…”

Section: Germinationsupporting

confidence: 87%

Microscopy of soybean seeds: cellular and subcellular structure during germination, development and processing with emphasis on lipid bodies

Bair

View full text Add to dashboard Cite

A Study of Protein Bodies During Germination of Peanut (Arachis Hypogaea) Seed

Cited by 55 publications

References 6 publications

Histochemical and Biochemical Observations on Storage Protein Metabolism and Protein Body Autolysis in Cotyledons of Germinating Mung Beans

Histochemical and Biochemical Observations on Storage Protein Metabolism and Protein Body Autolysis in Cotyledons of Germinating Mung Beans

Studies on Seeds

Microscopy of soybean seeds: cellular and subcellular structure during germination, development and processing with emphasis on lipid bodies

Contact Info

Product

Resources

About