The hybrid status of Spartina anglica (Poaceae). Enzymatic analysis of the species and of the presumed parents

1988 ◽  
Vol 66 (9) ◽  
pp. 1830-1833 ◽  
Author(s):  
M. C. Guenegou ◽  
J. Citharel ◽  
J. E. Levasseur
Keyword(s):  
Spartina Alterniflora ◽  
Hybrid Origin ◽  
Superoxide Dismutases ◽  
Acid Phosphatases ◽  
Enzymatic Analysis ◽  
Spartina Anglica ◽  
The West ◽  
Enzymatic Systems

Three enzymatic systems were analysed in Spartina alterniflora Loisel., S. maritima (Curt.) Fernald, and S. anglica C. E. Hubbard, using samples gathered in the west of France. Examination of the acid phosphatases, esterases, and superoxide dismutases demonstrates certain analogies found in the three species. The hypothesis of a hybrid origin for S. anglica remains probable and is indeed enhanced by the isoforms of the esterases.

scholarly journals Changes in protein content and activity of proteases and acid phosphatases in needles of Norway spruce (Picea abies L. Karst) seedlings treated with 2,4,5-T

2015 ◽  
Vol 44 (1) ◽  
pp. 41-49 ◽  
Author(s):  
Jan Tonecki
Keyword(s):  
Protein Content ◽  
Soluble Protein ◽  
Dry Matter ◽  
Protein Biosynthesis ◽  
Dry Matter Accumulation ◽  
Small Decrease ◽  
Acid Phosphatases ◽  
Soluble Protein Content ◽  
Enzymatic Systems ◽  
Intensive Growth

Effect of 2, 4, 5-T in different concentrations and time of herbicide applications on protein biosynthesis and enzymatic activity of proteases and acid phosphatases in needles of spruce seedlings was investigated. 2, 4, 5-T in all concentrations tested and applied on the seedlings during phase of intensive growth caused significant increase in soluble protein content. After spraying the seedlings with 100 and 300 mg ·l<sup>-1</sup> of 2, 4, 5-T before bud development a small decrease in soluble protein level was noted. The herbicide caused marked disturbances in the activity of enzymatic systems of proteases and acid phosphatases. No effect of 2, 4, 5-T on dry matter accumulation was observed.

scholarly journals Regulation of Key Antioxidant Enzymatic Systems in the Sheep Endometrium by Ovarian Steroids

Endocrinology ◽  
2008 ◽  
Vol 149 (9) ◽  
pp. 4428-4434 ◽  
Author(s):  
Kaïs H. Al-Gubory ◽  
Philippe Bolifraud ◽  
Catherine Garrel
Keyword(s):  
Superoxide Dismutases ◽  
Oxygen Species ◽  
Physiological Changes ◽  
Glandular Tissue ◽  
Female Reproductive System ◽  
Ovarian Steroids ◽  
Enzymatic Systems ◽  
Enzymatic Pathways ◽  
Firm Evidence

Reactive oxygen species (ROS) and their control by antioxidant enzymes are involved in the physiology of the female reproductive system. Thus, it is important to understand the regulation of key antioxidant enzymatic pathways. The roles of estrogen and progesterone in regulating the physiological functions of the endometrium have become central dogma. We examined the effects of ovarian steroids on superoxide dismutases (SOD1 and SOD2), catalase (CAT), glutathione peroxidase (GPX), and glutathione reductase (GSR) activities in the aglandular caruncular and glandular inter-caruncular endometrial tissues of ovariectomized (OVX) ewes and in OVX ewes treated with estradiol (E2), progesterone (P4), or both hormones according to schedules designed to produce physiological changes of these hormones during the estrous cycle. The activities SOD2, CAT, GPX and GSR in both endometrial tissues were unaffected by P4 treatment. The activity of SOD1 in the aglandular tissue was unaffected by P4 treatment, however this treatment decreased SOD1 activity in the glandular tissue (P &lt; 0.01). Treatment with E2, either alone or in combination with P4, decreased SOD1 (P &lt; 0.01), CAT (P &lt; 0.01) and GPX (P &lt; 0.05) activities in both endometrial tissues. The activity of GSR decreased only in the glandular tissue (P &lt; 0.05) after E2 treatment, either alone or in combination with P4. No change in SOD2 activity was detected in both endometrial tissues after administration of E2, P4 or both hormones. This study provides the first firm evidence for the role of ovarian steroid hormones in the regulation of the activities of key antioxidant enzyme in the endometrium of female mammals.

Inter-specific competition: Spartina alterniflora is replacing Spartina anglica in coastal China

2007 ◽  
Vol 74 (3) ◽  
pp. 437-448 ◽  
Author(s):  
Yingbiao Zhi ◽  
Hongli Li ◽  
Shuqing An ◽  
Lei Zhao ◽  
Changfang Zhou ◽  
...  
Keyword(s):  
Spartina Alterniflora ◽  
Spartina Anglica ◽  
Coastal China

Enumeration and Identification of Asbestos Fibres in Water

1974 ◽  
Vol 32 ◽  
pp. 526-527 ◽  
Author(s):  
O. Mudroch ◽  
J. R. Kramer
Keyword(s):  
Water Supply ◽  
Water Samples ◽  
Drainage Basin ◽  
Lake Superior ◽  
Research Work ◽  
List Type ◽  
The West ◽  
Asbestos Fibre ◽  
Amphibole Asbestos

Approximately 60,000 tons per day of waste from taconite mining, tailing, are added to the west arm of Lake Superior at Silver Bay. Tailings contain nearly the same amount of quartz and amphibole asbestos, cummingtonite and actinolite in fibrous form. Cummingtonite fibres from 0.01μm in length have been found in the water supply for Minnesota municipalities.The purpose of the research work was to develop a method for asbestos fibre counts and identification in water and apply it for the enumeration of fibres in water samples collected(a) at various stations in Lake Superior at two depth: lm and at the bottom.(b) from various rivers in Lake Superior Drainage Basin.

Localization of acid phosphatases in root cap of rice plant

1991 ◽  
Vol 49 ◽  
pp. 224-225
Author(s):  
Y. R. Chen ◽  
Y. F. Huang ◽  
W. S. Chen
Keyword(s):  
Rice Plant ◽  
Developmental Stages ◽  
Uranyl Acetate ◽  
Root Cap ◽  
Plant Tissues ◽  
Acid Phosphatases ◽  
Root Tips ◽  
Buffer Solution ◽  
Cacodylate Buffer ◽  
Ethanol Series

Acid phosphatases are widely distributed in different tisssues of various plants. Studies on subcellular localization of acid phosphatases show they might be present in cell wall, plasma lemma, mitochondria, plastid, vacuole and nucleus. However, their localization in rice cell varies with developmental stages of cells and plant tissues. In present study, acid phosphatases occurring in root cap are examined.Sliced root tips of ten-day-old rice(Oryza sativa) seedlings were fixed in 0.1M cacodylate buffer containing 2.5% glutaraldehyde for 2h, washed overnight in same buffer solution, incubated in Gomori's solution at 37° C for 90min, post-fixed in OsO4, dehydrated in ethanol series and finally embeded in Spurr's resin. Sections were doubly stained with uranyl acetate and lead citrate, and observed under Hitachi H-600 at 75 KV.

The Demonstration of Human Prostatic Acid Phosphatase (Pap) With Phosphorylcholine

1976 ◽  
Vol 34 ◽  
pp. 88-89
Author(s):  
José A. Serrano ◽  
Hannah L. Wasserkrug ◽  
Anna A. Serrano ◽  
Arnold M. Seligman
Keyword(s):  
Acid Phosphatase ◽  
Prostate Gland ◽  
Prostatic Acid Phosphatase ◽  
Human Prostate ◽  
Rat Tissues ◽  
Specific Substrate ◽  
Acid Phosphatases ◽  
Lysosomal Acid ◽  
Cacodylate Buffer

As previously reported (1, 2) phosphorylcholine (PC) is a specific substrate for prostatatic acid phosphatase (PAP) as opposed to other acid phosphatases, e.g., lysosomal acid phosphatase. The specificity of PC for PAP is due to the pentavalent nitrogen in PC, a feature that renders PC resistant to hydrolysis by all other acid phosphatases. Detailed comparative cytochemical results in rat tissues are in press. This report deals with ultracytochemical results applying the method to normal and pathological human prostate gland.Fresh human prostate was obtained from 7 patients having transurethral resections or radical prostatectomies. The tissue was fixed in 3% glutaraldehyde- 0.1 M cacodylate buffer (pH 7.4) for 15 min, sectioned at 50 μm on a Sorvall TC-2 tissue sectioner, refixed for a total of 2 hr, and rinsed overnight in 0.1 M cacodylate buffer (pH 7.4)-7.5% sucrose.

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