Intracellular Localization of Acid Peptide Hydrolases and Several Other Acid Hydrolases in the Leaf of Pea (Pisum sativum L.)

1982 ◽  
Vol 9 (3) ◽  
pp. 353 ◽  
Author(s):  
ER Noble ◽  
MJ Dalling
Keyword(s):  
Crude Extract ◽  
Intracellular Localization ◽  
Acid Proteinase ◽  
Phenylmethylsulfonyl Fluoride ◽  
Acid Hydrolases ◽  
Pisum Sativum L ◽  
Acid Carboxypeptidase ◽  
Digestion Mixture ◽  
Protoplast Preparation ◽  
Peptide Hydrolases

Protoplasts and vacuoles were prepared from pea (P. sativum L.) leaves to determine the acid-hydrolase content of the vacuole. The protoplasts and vacuoles were isolated on sucrose-sorbitol gradients. We conclude that the protoplast preparation was free of enzyme contamination arising from the digestion mixture, after comparing the specific activities of the crude extract and of the isolated protoplasts, and the response to the thiol inhibitor p-chloromercuribenzoate of the crude extract and protoplast acid proteinase with that of the Cellulysin enzyme. N-acetyl-β-D-glucosaminidase, α-mannosidase, acid carboxypeptidase and acid proteinase appeared to be located entirely in the vacuole. Approximately 60% of the acid-phosphatase and 27% of the phosphodiesterase activities were found in the vacuole. We conclude that the acid proteinase and the acid carboxypeptidase are separate enzymes in pea leaves, based on their different sensitivities to the inhibitors phenylmethylsulfonyl fluoride and p-chloromercuribenzoate.

scholarly journals Purification of human renin by affinity chromatography using a new peptide inhibitor of renin, H.77 (D-His-Pro-Phe-His-Leu-R-Leu-Val-Tyr)

1983 ◽  
Vol 211 (2) ◽  
pp. 519-522 ◽  
Author(s):  
G D McIntyre ◽  
B Leckie ◽  
A Hallett ◽  
M Szelke
Keyword(s):  
Crude Extract ◽  
Specific Activity ◽  
Human Kidney ◽  
Peptide Inhibitor ◽  
Kidney Cortex ◽  
Affinity Column ◽  
Acid Proteinase ◽  
Human Renin ◽  
Enzyme Specific Activity ◽  
Sepharose 4B

A new affinity column for renin was prepared by coupling the isosteric peptide inhibitor of renin, H.77 (D-His-Pro-Phe-His-LeuR-Leu-Val-Tyr, where R is a reduced isosteric bond, -CH2-NH-), to activated 6-aminohexanoic acid-Sepharose 4B. Chromatography of a crude extract of human kidney cortex on this material resulted in a 5500-fold purification of renin in 76% yield. The purified enzyme (specific activity 871 units/mg) was free of non-specific acid-proteinase activity and was stable at pH 6.8 and −20 degrees C over a period of several weeks.

scholarly journals Proteome Map of Pea (Pisum Sativum L.) Embryos Containing Different Amounts of Residual Chlorophylls

2018 ◽  
Author(s):  
Tatiana Mamontova ◽  
Elena Lukasheva ◽  
Gregory Mavropolo-Stolyarenko ◽  
Carsten Proksch ◽  
Tatiana Bilova ◽  
...  
Keyword(s):  
Pisum Sativum ◽  
Seed Protein ◽  
High Efficiency ◽  
Animal Feed ◽  
Intracellular Localization ◽  
Food Protein ◽  
Protein Patterns ◽  
Pisum Sativum L ◽  
Pea Seeds ◽  
Pea Seed

Due to low culturing costs and high seed protein contents, legumes represent the main global source of food protein. Pea (Pisum sativum L.) is one of the major economically important legume crops, impacting both animal feed and human nutrition. Therefore, the quality of pea seeds needs to be ensured in the context of sustainable crop production and nutritional efficiency. Obviously, changes in seed protein patterns might directly affect both of these aspects. Thus, here we address the pea seed proteome in more detail and provide, to the best of our knowledge, the most comprehensive annotation of the functions and intracellular localization of pea seed proteins. Accordingly, 1938 and 1989 non-redundant proteins were identified in yellow and green pea seeds, in total. Only 35 and 44 proteins, respectively, could be additionally identified after protamine sulfate precipitation (PSP) potentially indicating the high efficiency of our experimental workflow. In total 981 protein groups could be assigned to 34 functional classes, which were to a large extent differentially represented in yellow and green seeds. Closer analysis of these differences by processing of the data in KEGG and String databases revealed their possible relation to a higher metabolic status and reduced longevity of green seeds.

scholarly journals Intracellular Localization of Peptide Hydrolases in Wheat (Triticum aestivum L.) Leaves

1982 ◽  
Vol 69 (3) ◽  
pp. 575-579 ◽  
Author(s):  
Stephen P. Waters ◽  
Elaine R. Noble ◽  
Michael J. Dalling
Keyword(s):  
Triticum Aestivum ◽  
Intracellular Localization ◽  
Triticum Aestivum L ◽  
Peptide Hydrolases

scholarly journals Proteome Map of Pea (Pisum sativum L.) Embryos Containing Different Amounts of Residual Chlorophylls

2018 ◽  
Vol 19 (12) ◽  
pp. 4066 ◽  
Author(s):  
Tatiana Mamontova ◽  
Elena Lukasheva ◽  
Gregory Mavropolo-Stolyarenko ◽  
Carsten Proksch ◽  
Tatiana Bilova ◽  
...  
Keyword(s):  
Pisum Sativum ◽  
Crop Production ◽  
Seed Protein ◽  
High Efficiency ◽  
Animal Feed ◽  
Intracellular Localization ◽  
Food Protein ◽  
Protein Patterns ◽  
Pisum Sativum L ◽  
Pea Seed

Due to low culturing costs and high seed protein contents, legumes represent the main global source of food protein. Pea (Pisum sativum L.) is one of the major legume crops, impacting both animal feed and human nutrition. Therefore, the quality of pea seeds needs to be ensured in the context of sustainable crop production and nutritional efficiency. Apparently, changes in seed protein patterns might directly affect both of these aspects. Thus, here, we address the pea seed proteome in detail and provide, to the best of our knowledge, the most comprehensive annotation of the functions and intracellular localization of pea seed proteins. To address possible intercultivar differences, we compared seed proteomes of yellow- and green-seeded pea cultivars in a comprehensive case study. The analysis revealed totally 1938 and 1989 nonredundant proteins, respectively. Only 35 and 44 proteins, respectively, could be additionally identified after protamine sulfate precipitation (PSP), potentially indicating the high efficiency of our experimental workflow. Totally 981 protein groups were assigned to 34 functional classes, which were to a large extent differentially represented in yellow and green seeds. Closer analysis of these differences by processing of the data in KEGG and String databases revealed their possible relation to a higher metabolic status and reduced longevity of green seeds.

scholarly journals Proteome Map of Pea (Pisum Sativum L.) Embryos Containing Different Amounts of Residual Chlorophylls

2018 ◽  
Author(s):  
Tatiana Mamontova ◽  
Elena Lukasheva ◽  
Gregory Mavropolo-Stolyarenko ◽  
Carsten Proksch ◽  
Tatiana Bilova ◽  
...  
Keyword(s):  
Pisum Sativum ◽  
Seed Protein ◽  
High Efficiency ◽  
Animal Feed ◽  
Intracellular Localization ◽  
Food Protein ◽  
Protein Patterns ◽  
Pisum Sativum L ◽  
Pea Seeds ◽  
Pea Seed

Due to low culturing costs and high seed protein contents, legumes represent the main global source of food protein. Pea (Pisum sativum L.) is one of the major economically important legume crops, impacting both animal feed and human nutrition. Therefore, the quality of pea seeds needs to be ensured in the context of sustainable crop production and nutritional efficiency. Obviously, changes in seed protein patterns might directly affect both of these aspects. Thus, here we address the pea seed proteome in more detail and provide, to the best of our knowledge, the most comprehensive annotation of the functions and intracellular localization of pea seed proteins. Accordingly, 1938 and 1989 non-redundant proteins were identified in yellow and green pea seeds, in total. Only 35 and 44 proteins, respectively, could be additionally identified after protamine sulfate precipitation (PSP) potentially indicating the high efficiency of our experimental workflow. In total 981 protein groups could be assigned to 34 functional classes, which were to a large extent differentially represented in yellow and green seeds. Closer analysis of these differences by processing of the data in KEGG and String databases revealed their possible relation to a higher metabolic status and reduced longevity of green seeds.

The Morphology of the Rat Kidney Following Folic Acid Administration

1970 ◽  
Vol 28 ◽  
pp. 200-201
Author(s):  
Aline Byrnes ◽  
Elsa E. Ramos ◽  
Minoru Suzuki ◽  
E.D. Mayfield
Keyword(s):  
Folic Acid ◽  
De Novo ◽  
Specific Activity ◽  
Rat Kidney ◽  
Present Report ◽  
Intracellular Localization ◽  
Male Rats ◽  
Renal Hypertrophy ◽  
Electron Microscopic ◽  
Biochemical Alterations

Renal hypertrophy was induced in 100 g male rats by the injection of 250 mg folic acid (FA) dissolved in 0.3 M NaHCO3/kg body weight (i.v.). Preliminary studies of the biochemical alterations in ribonucleic acid (RNA) metabolism of the renal tissue have been reported recently (1). They are: RNA content and concentration, orotic acid-c14 incorporation into RNA and acid soluble nucleotide pool, intracellular localization of the newly synthesized RNA, and the specific activity of enzymes of the de novo pyrimidine biosynthesis pathway. The present report describes the light and electron microscopic observations in these animals. For light microscopy, kidney slices were fixed in formalin, embedded, sectioned, and stained with H & E and PAS.

The Immuno-Electron Microscopic Localization of the Mo-Fe Protein Component of Nitrogenase in Cells of Azotobacter Vinelandii

1973 ◽  
Vol 31 ◽  
pp. 574-575
Author(s):  
J. T. Stasny ◽  
R. C. Burns ◽  
R. W. F. Hardy
Keyword(s):  
Cellular Localization ◽  
Direct Evidence ◽  
Azotobacter Vinelandii ◽  
Intracellular Localization ◽  
Protein Component ◽  
Electron Microscopic ◽  
Thin Sections ◽  
Fe Protein ◽  
Intracytoplasmic Membranes

Structure-functlon studies of biological N2-fixation have correlated the presence of the enzyme nitrogenase with increased numbers of intracytoplasmic membranes in Azotobacter. However no direct evidence has been provided for the internal cellular localization of any nitrogenase. Recent advances concerned with the crystallizatiorTand the electron microscopic characterization of the Mo-Fe protein component of Azotobacter nitrogenase, prompted the use of this purified protein to obtain antibodies (Ab) to be conjugated to electron dense markers for the intracellular localization of the protein by electron microscopy. The present study describes the use of ferritin conjugated to goat antitMo-Fe protein immunoglobulin (IgG) and the observations following its topical application to thin sections of N2-grown Azotobacter.

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