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2.
J Environ Sci Eng ; 53(3): 365-70, 2011 Jul.
Article in English | MEDLINE | ID: mdl-23029939

ABSTRACT

Our objective was to carry out environmental impact assessment of small scale industries in Kashmir (India). A prepared questionnaire was circulated among the workers, owners and residents to assess the pros and cons of the small scale industries in Kashmir. The study revealed that most of the small scale industries in Kashmir valley have an impact on the quality of the environment and may cause discomfort to the people living very close to these industries. It has been observed that small scale industries lack efficient waste management system. However, the generated wastes from these units may be used effectively, as a raw material in various ways when managed properly and may minimize the impact on the quality of the environment and may also contribute in improving the economy of the State. The proliferation of small scale industries has caused an irreversible damage to the agricultural land of the area studied.


Subject(s)
Environment , Environmental Monitoring/methods , Waste Management/methods , Agriculture , Climate , Environmental Health , Environmental Pollution/prevention & control , Forestry , Geography , Humans , Humidity , India , Industrial Waste , Industry , Occupational Health , Social Class , Temperature , Waste Disposal, Fluid
3.
Arch Androl ; 33(1): 23-9, 1994.
Article in English | MEDLINE | ID: mdl-7979806

ABSTRACT

Human seminal plasma (hsp) contains soluble proteins capable of binding immunoglobulin (Ig) G. Two novel components with estimated molecular sizes of 90 and 21 kD interact specifically with a variant of IgG2 found in 20% of human sera tested. The common IgG2 present in human sera and other subclasses of IgG did not bind with the hsp components. The present findings shows that the interacting IgG2 is a variant and not the common or prevalent species. The 90-kD component of hsp with IgG2 binding property is probably a nonglycosylated protein, whereas the 21-kD component is a glycosylated protein. The 90- and 21-kD components were detected in 20% of hsp specimens tested. Thus they are not present in the majority of hsp. Since the IgG2 binding components of hsp and the serum IgG2 variant are found in 20% of men and 20% of individuals, respectively, they can be used as genetic markers.


Subject(s)
Genetic Variation , Glycoproteins/isolation & purification , Heat-Shock Proteins/isolation & purification , Immunoglobulin G/metabolism , Semen/immunology , Antibodies, Monoclonal , Blotting, Western , Electrophoresis, Polyacrylamide Gel , Glycoproteins/immunology , Heat-Shock Proteins/metabolism , Humans , Immunoglobulin G/classification , Immunoglobulin G/genetics , Male , Molecular Weight
4.
Arch Androl ; 32(3): 219-25, 1994.
Article in English | MEDLINE | ID: mdl-8074577

ABSTRACT

Human seminal plasma contains a factor that binds human immunoglobulin G (IgG). The factor has an estimated M(r) of 50 kD and interacts specifically with human IgG4. It does not bind other subclasses of human IgG or IgGs of other mammalian species tested. The factor was purified by affinity chromatography on protein G column. The 50-kD component was eluted in the adsorbed fraction and immunostained with monoclonal antibodies against heavy chain (gamma) of IgG. Purified subclasses of human serum IgG were separated into heavy and light chains by sodium dodecyl sulfate polyacrylamide gel electrophoresis under reduced condition. The heavy chains of all subclasses of IgG bound IgG4. The present findings suggest that the 50-kD IgG4 binding factor of human seminal plasma is the heavy chain of IgG.


Subject(s)
Immunoglobulin Heavy Chains/analysis , Lymphokines/analysis , Prostatic Secretory Proteins , Semen/chemistry , Suppressor Factors, Immunologic/analysis , Animals , Humans , Molecular Weight , Species Specificity
5.
Res Commun Chem Pathol Pharmacol ; 84(1): 3-15, 1994 Apr.
Article in English | MEDLINE | ID: mdl-8042007

ABSTRACT

The nucleotide sequence of the cDNA encoding a sperm protein (rSMP-B) was determined in a previous study. Two peptide segments corresponding to the extracellular domain of the deduced sperm polypeptide were synthesized as multiple antigen peptide (MAP) and designated as rSMP-229 and rSMP-230. Polyclonal antibodies were raised against the two MAPs. Sera obtained from rabbits immunized with rSMP-230 interacted with human and rabbit sperm membrane proteins with estimated molecular sizes of 72 and 20.1 kD, respectively. Adult female and male rats were immunized with the MAPs and their fertilities determined. Immunization of female rats with rSMP-229 and rSMP-230 induced infertility in 25% and 83% of the treated animals, respectively. All male rats immunized with rSMP-229 remained fertile; whereas animals immunized with rSMP-230 did not mate with normal cycling female rats. Three impotent male rats were found to regain their mating potency 45 days after the last booster injection. These findings demonstrated that immunization with rSMP-230 induced a reversible impotency in male rats. Serum testosterone and LH levels were reduced in rSMP-230-immunized male rats and were elevated in rSMP-229-immunized animals. Histopathological examination of sections of testes from male rats immunized with rSMP-230 showed impairment of spermatogenesis and sloughing of germ cells into the lumen of the seminiferous tubules. The testes of male rats immunized with rSMP-229 showed normal morphology and active spermatogenesis with scattered foci of nodular hyperplasia of Leydig cells in the interstitial areas. In conclusion, immunization with synthetic peptide segments corresponding to different domains of a deduced sperm protein induced infertility in a significant number of female rats and transient impotency in male rats.


Subject(s)
Antigens, Surface , Immunization , Infertility/immunology , Membrane Proteins/immunology , Peptide Fragments/immunology , Spermatozoa/immunology , Amino Acid Sequence , Animals , Female , Follicle Stimulating Hormone/blood , Humans , Immune Sera , Immunoblotting , Luteinizing Hormone/blood , Male , Membrane Proteins/chemical synthesis , Membrane Proteins/chemistry , Molecular Sequence Data , Peptide Fragments/chemical synthesis , Peptide Fragments/chemistry , Rabbits , Rats , Rats, Sprague-Dawley , Testis/immunology , Testis/pathology , Testosterone/blood
6.
Biochem Biophys Res Commun ; 168(1): 71-7, 1990 Apr 16.
Article in English | MEDLINE | ID: mdl-2328014

ABSTRACT

The steady-state levels of mRNA and transcription of alpha-skeletal actin (alpha-SKA) and adult myosin heavy chain (MHC) genes were measured in the skeletal, cardiac and uterine muscles of young (22-25 week) and old (123-135 week) female rats. The effects of 10(-8) M 17 beta-estradiol/dexamethasone/T3 alpha on their transcription were also studied. The data show that the alpha-SKA mRNA level is lower in the old skeletal muscle and uterus, but is higher in the old myocardium. The adult MHC mRNA level is not different in the three muscles of both the ages. The transcription of alpha-SKA gene is lower in the skeletal muscle and higher in the uterus of old rats. It is unaltered in the myocardium of old rats. The transcription of adult MHC gene is lower in the old uterus. The effects of hormones on transcription of both the genes are different in the three muscles. We show that the expression of alpha-SKA gene is tissue-specific and age-related. The over-expression of alpha-SKA gene in the old myocardium is possibly due to derepression of the gene caused by hypertrophy of cardiac myocytes, and continuous hemodynamic pressure overload on the old heart.


Subject(s)
Actins/genetics , Aging , Muscles/physiology , Myosins/genetics , Animals , Dexamethasone/pharmacology , Estradiol/pharmacology , Female , Gene Expression , Heart/physiology , In Vitro Techniques , Muscle, Smooth/physiology , RNA, Messenger/genetics , Rats , Tissue Distribution , Transcription, Genetic/drug effects , Triiodothyronine/pharmacology , Uterus/physiology
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