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.

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.

scholarly journals HISTOCHEMICAL STUDIES OF MITOCHONDRIAL VARIATION DURING AEROBIC GROWTH OF RESPIRATION-NORMAL BAKER'S YEAST

1965 ◽  
Vol 13 (5) ◽  
pp. 344-349 ◽  
Author(s):  
C. J. AVERS ◽  
F. H. LIN ◽  
C. R. PFEFFER
Keyword(s):  
Cytochrome Oxidase ◽  
Succinic Dehydrogenase ◽  
Growth Cycle ◽  
Autonomous Control ◽  
Mitochondrial Enzyme ◽  
Aerobic Growth ◽  
Acceleration Phase ◽  
Enzyme Systems ◽  
Zero Values ◽  
The Common

Histochemical localizations of cytochrome oxidase, succinic dehydrogenase, DPNH-tetrazolium reductase, and TPNH-tetrazolium reductase activities revealed at least two kinds of mitochondria in the intracellular population. The total chondriome in stationary phase cells contains about 45 mitochondria, all with cytochrome oxidase activity. But, only about 30 mitochondria per cell were active for dehydrogenase or reductases. The differences in mitochondrial enzyme activities persisted throughout the growth cycle, showing different numbers of active mitochondria and different rates of their increase and decrease for all four enzyme systems. Manometric data verified the differences between cytochrome oxidase and succinic dehydrogenase for the earlier phases of the growth cycle. In histochemical counts, zero values for all four enzymes occurred in late acceleration phase, but persisted into log phase only for the tetrazolium reductases. Both cytochrome oxidase- and succinic dehydrogenase-active mitochondria began to increase in numbers at the inception of log phase, but at very different rates. The demonstration of more than one kind of mitochondrion in the common nucleocytoplasmic system of a single cell was considered to be evidence of some measure of autonomous control of the mitochondrial phenotype.

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.

Effect of mercuric chloride on some kidney enzymes in chow-fed and sucrose-fed rats

1960 ◽  
Vol 198 (1) ◽  
pp. 187-190 ◽  
Author(s):  
V. Shore ◽  
B. Shore
Keyword(s):  
Alkaline Phosphatase ◽  
Cytochrome Oxidase ◽  
Mercuric Chloride ◽  
Tricarboxylic Acid Cycle ◽  
Succinic Dehydrogenase ◽  
Tricarboxylic Acid ◽  
Acid Cycle ◽  
Enzyme Systems ◽  
Rat Kidneys ◽  
Ketoglutarate Dehydrogenase

Rats given a diet of sucrose and vitamins for 3 weeks or more develop a tolerance to mercuric chloride greater than that of chow-fed rats. Comparison of several enzyme systems (tricarboxylic acid cycle, succinic dehydrogenase, cytochrome oxidase, α-ketoglutarate dehydrogenase, alkaline phosphatase, cathepsins and ß-glucuronidase) in chow-fed and sucrose-fed rats indicated no significant differences in activities. After 3 mg HgCl2/kg i.v., notable differences in the extent of inhibition of tricarboxylic acid enzyme systems were observed. Twenty-four hours after such an injection, kidneys of chow-fed rats were seriously hampered in their ability to perform biological energy transformations. Oxidation and phosphorylation by sucrose-fed rat kidneys were considerably less inhibited.

scholarly journals STUDIES ON THE MECHANISM OF HYDROGEN TRANSPORT IN ANIMAL TISSUES

1943 ◽  
Vol 26 (5) ◽  
pp. 443-455 ◽  
Author(s):  
V. R. Potter ◽  
H. G. Albaum
Keyword(s):  
Alkaline Phosphatase ◽  
Cytochrome C ◽  
Xanthine Oxidase ◽  
Cytochrome Oxidase ◽  
Adenosine Triphosphatase ◽  
Succinic Dehydrogenase ◽  
Hydrogen Transport ◽  
Animal Tissues ◽  
Cytochrome C Reductase ◽  
Enzyme Systems

1. The effect of ribonuclease on various enzyme systems was studied as one approach to the problem of whether or not these enzymes are contained in macromolecules of ribonucleoprotein nature in protoplasm. 2. Ribonuclease inhibited CoI-cytochrome c reductase, succinic dehydrogenase, and cytochrome oxidase, all of which require cytochrome c in order to function. Ribonuclease did not act on cytochrome c. 3. Ribonuclease did not inhibit urease, xanthine oxidase, catalase, alkaline phosphatase, or adenosine triphosphatase under the conditions employed. 4. It was suggested that ribonuclease acted sterically by preventing contact between cytochrome c and its activating centers. 5. It was suggested that the enzymes inhibited may be contained in a ribonucleoprotein of macromolecular dimensions but that the enzymes not inhibited are not necessarily excluded from such a complex by the data presented. 6. Further evidence against the Szent-Györgyi theory of hydrogen transport was presented and discussed.

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