A histochemical study of starch, lipids, and certain enzymes in senescing rose stems

1977 ◽  
Vol 55 (6) ◽  
pp. 617-624 ◽  
Author(s):  
J. M. Molnar ◽  
E. V. Parups
Keyword(s):  
Acid Phosphatase ◽  
Cytochrome Oxidase ◽  
Lipid Content ◽  
Histochemical Study ◽  
Succinic Dehydrogenase ◽  
Sugar Solution ◽  
Lipid Peroxidase ◽  
High Level ◽  
The Rose ◽  
Cut Rose

The starch, lipid, cytochrome oxidase (EC 1.9.3.1), succinic dehydrogenase (EC 1.3.99.1), peroxidase (EC 1.11.1.7), and acid phosphatase (EC 3.1.3.2) levels were determined periodically by histochemical methods in transverse sections of cut stem of the rose, Rosa hybrida L. cv. Forever Yours, kept in water or in an aqueous preservative solution containing 4% sucrose, 100 ppm sodium isoascorbate, and 100 ppm 8-hydroxyquinoline sulfate. Senescence of the cutrose stem, including leaves and flowers, was delayed by use of the sugar solution. The levels of cytochrome oxidase and succinic dehydrogenase were not significantly affected by either of the treatments. Starch, lipid, peroxidase, and acid phosphatase levels decreased in the tissues of rapidly senescing stems kept in water. In tissues where senescence was retarded by use of sugar solutions the lipid content and peroxidase were maintained at a relatively high level; starch, and acid phosphatase levels steadily increased. It is suggested that in cut rose stems, the onset or retardation of senescence is not related to the activities of acid phosphatase or peroxidase.

A histochemical study of the shoot apical meristem of Rauwolfia with reference to differentiation of sclereids

1968 ◽  
Vol 46 (2) ◽  
pp. 115-120 ◽  
Author(s):  
Abdul J. Mia ◽  
Suman M. Pathak
Keyword(s):  
Acid Phosphatase ◽  
Cytochrome Oxidase ◽  
Apical Meristem ◽  
Histochemical Study ◽  
Enzymatic Reaction ◽  
Succinic Dehydrogenase ◽  
Enzyme Systems ◽  
Strong Positive Reaction ◽  
Parenchyma Cells ◽  
Pith Parenchyma

The Rauwolfia apical meristem has three zones which are cytologically recognizable, viz. tunica, corpus, and pith-cell meristem. Histochemically, however, these zonations are not discernible. The entire meristem either reacts positively or negatively for a particular enzyme. The apical meristem and procambial strands give a strong positive reaction for cytochrome oxidase, succinic dehydrogenase, and total protein. The pith cells react positively with peroxidase, acid phosphatase, and phosphorylase. Alkaline phosphatase is distributed throughout the meristematic and non-meristematic areas of the shoot apex. Cells in these areas appear to give slight reaction for glucose-6-phosphatase and 5-nucleotidase. Activities of several enzyme systems, such as cytochrome oxidase, peroxidase, succinic dehydrogenase, and acid phosphatase, were localized in the sclereid initials. Commonly the sclereids give more intensified enzymatic reaction than the pith parenchyma cells.

scholarly journals A HISTOCHEMICAL STUDY OF PHAGOCYTIC AND ENZYMATIC FUNCTIONS OF RABBIT MONONUCLEAR AND POLYMORPHONUCLEAR EXUDATE CELLS AND ALVEOLAR MACROPHAGES

1963 ◽  
Vol 17 (3) ◽  
pp. 465-486 ◽  
Author(s):  
Arthur M. Dannenberg ◽  
Marvin S. Burstone ◽  
Paul C. Walter ◽  
June W. Kinsley
Keyword(s):  
Alkaline Phosphatase ◽  
Acid Phosphatase ◽  
Alveolar Macrophages ◽  
Histochemical Study ◽  
Succinic Dehydrogenase ◽  
Enzymatic Activities ◽  
Dust Particles ◽  
Cell Type ◽  
Microbial Agents

The cytochrome oxidase (CO), aminopeptidase (AMP), succinic dehydrogenase (SD), acid phosphatase, esterase, and alkaline phosphatase of rabbit mononuclear (MN) and polymorphonuclear (PMN) peritoneal exudate cells and pulmonary alveolar macrophages (AM) - air dried on Mylar strips - were characterized by histochemical techniques with respect to stability, activators, inhibitors, and pH optima. A granule count method was established for the quantitation of these enzymes. For the acid phosphatase of MN, in which the most precise results were obtained, time, pH, substrate, and inhibitor curves resembled those commonly obtained biochemically. Five of these enzymes were usually more active in AM than MN, whereas the sixth, alkaline phosphatase, was not present in either cell type. AM also tended to consume more oxygen than MN and to divide more frequently. Since the most active cells in the population would be first involved in the host's defense against microbial agents, a comparison was made of the 10 per cent of the AM and MN with the highest enzymatic activities. No differences were found in the granule counts that were not reflected by the means. However, within a given AM population, cells containing ingested dust particles seemed to have higher enzymatic activities than those without particles. MN had greater acid phosphatase and SD activities than PMN and consumed more oxygen, but the CO, AMP, and esterase activites of both types of cells were of similar magnitude. PMN showed high alkaline phosphatase activity; MN showed none. A survey of the histochemical literature indicates that a positive correlation between the enzymatic and phagocytic activities of both MN and PMN exists in vivo.

Effects of Kanwa on Rat Gastrointestinal Phosphatases

2010 ◽  
Vol 3 (3) ◽  
pp. 1147-1152
Author(s):  
Jacob Bamaiyi ◽  
Omajali ◽  
Sanni Momoh
Keyword(s):  
Alkaline Phosphatase ◽  
Small Intestine ◽  
Acid Phosphatase ◽  
Sodium Carbonate ◽  
Elevated Level ◽  
Food Additive ◽  
Alkaline Phosphatases ◽  
Acid And Alkaline Phosphatases ◽  
Diagnostic Indices ◽  
High Level

This study investigates the effects of kanwa on rat gastrointestinal phosphatases. The rats were administered 7% w/v concentration of  trona (Kanwa) orally for a period of two weeks in order to investigate how this compound is being used as food additive in some homes in Nigeria. The Kanwa used in this study was the handpicked variety obtained from sellers from Anyigba market in eastern part of Kogi State, Nigeria. Kanwa, a hydrated sodium carbonate (Na2CO3NaHCO3.2H2O) was obtained as a dried lake salt. Acid phosphatase has the ability to dephosphorylate molecules containing phosphate group. The decreased and elevated level in serum or plasma acid and alkaline phosphatases serves as diagnostic indices for various diseases. Results showed that there was increase and decrease of acid phosphatase (ACP) activities in both the stomach and small intestine. The activities of alkaline phosphatase (ALP) fluctuated in the small intestine. However, in the stomach, an increase activity of ALP was noticed throughout the period of ‘Kanwa’ administration. We concluded that although the level of ‘Kanwa’ consumed in most homes may not be toxic if not taken continuously or repeatedly. Thus, continuous consumption should be discouraged as accumulation of high level of ‘Kanwa’ may cause damages or injuries to the various organs/tissues and may disrupt normal body function.

Oxidative Activity of Aortic Tissue of Man, the Rabbit and the Dog, With Special Reference to Succinic Dehydrogenase and Cytochrome Oxidase

1958 ◽  
Vol 195 (2) ◽  
pp. 476-480 ◽  
Author(s):  
Nelicia Maier ◽  
Henry Haimovici
Keyword(s):  
Special Reference ◽  
Cytochrome Oxidase ◽  
Abdominal Aorta ◽  
Abdominal Segment ◽  
Species Difference ◽  
Succinic Dehydrogenase ◽  
Hepatic Tissue ◽  
Human Aorta ◽  
Aortic Tissue ◽  
Enzymatic Systems

Succinic dehydrogenase and cytochrome oxidase activities were determined in homogenates of three aortic segments (ascending and arch, descending thoracic, abdominal) and liver of man, the rabbit and the dog. Both enzymes exhibited the lowest activity in human aorta. Succinic dehydrogenase exhibited the highest activity in the thoracic aorta of the dog and intermediate activity in the latter's abdominal segment and the rabbit's aorta. Cytochrome oxidase, in contrast, exhibited the highest activity in the rabbit's aorta. A slight gradient of decreasing activity from thoracic to abdominal aorta was noted for cytochrome oxidase in both the rabbit and dog and for succinic dehydrogenase in the rabbit, whereas a significant decrease in the latter enzyme was noted in the abdominal segment of the dog. No gradient of activity was apparent in man. Liver exhibited the lowest activity for both enzymes in man, highest in the dog and intermediate in the rabbit. The above findings suggest a biologic species difference between the aorta of man, the rabbit and the dog, which may be partly ascribed to a difference in the components of the above two enzymatic systems. The same species difference holds true for hepatic tissue.

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