2 edition of Biochemical studies on the human cataractous lens. found in the catalog.
Biochemical studies on the human cataractous lens.
John Funsho Alao
PhD thesis, Chemistry.
Biochemical evidence is presented for the disintegration of the lens fiber plasma membrane in human cataracts. The intrinsic membrane proteins are found in both the water-soluble and water. Biochemical Studies on the Human Cataractous Lens. Author: Alao, J. F. ISNI: Awarding Body: University of Salford Current Institution: University of Salford Date of Award: Availability of Full Text: Full text unavailable from EThOS.
Bettelheim FA, Chylack LT. Light scattering of whole excised human cataractous lenses: relationship between different light scattering parameters. Exp Eye Res . The purpose of the study was to examine the zinc and iron content of human lenses in different types of cataract and to investigate the possible influence of diabetes on the zinc and iron content of the lens. Iron and zinc of 57 human lenses (28 corticonuclear cataracts and 29 mature cataracts with a mean age of ± and ± yr,
The nucleus of the cataractous lens (core part of the human lens) from operated cases first examined for colour and then transferred in dry state to the laboratory for biochemical assay of. studies on human lenses: ii. distribution and solubility of fluorescent pigments in cataractous and non-cataractous lenses of indian origin. photochemistry and photobiology , 55 (5), doi: /jtbx.
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Removing the lens epithelium and capsule leads to progression of the cataractous changes in the human lens. Thus, in this study, the progression of the cataract was noted in both the lanosterol group and control group.
Different biochemical changes in the lens both in vivo and in vitro would have an effect on the : Ramesh Venkatesh, Prachi Gurav, Shailja Tibrewal. Abstract. Biochemical evidence is presented for the disintegration of the lens fiber plasma membrane in human cataracts.
The intrinsic membrane proteins are found in both the water-soluble and water-insoluble nonmembrane fractions of the cataract lens but not in the normal by: Background: Cataract is one of the major causes of a visual impairment, which eventually leads to blindness. An oxidative damage to the lens proteins is a major factor which leads to cataract formation.
Therefore, we intended to study the relationship between the biochemical markers of oxidative stress and various forms of by: Biochemical studies on cataractous human lenses. (PMID) Abstract Citations; Related Articles; Data; BioEntities; External Links ' ' Rawal UM, ' ' Patel US, ' ' Desai RJ The Indian Journal of Medical Research [01 Jan] Type: Journal Article.
Abstract. No Cited by: 8. Comparative Study of Enzymes in Normal and Cataractous Human Lens Ajit V Pandya* C U Shah Science College, Ahmedabad.
Received 16th September ; Accepted 25th November ; Available on line December ABSTRACT: Cataract is referred as opacity of lens due to multi factorial etiology.
All the constituents of the protecting. WATER CONTENT AND SOLIDS OF CATARACTOUS AND SCLEROSED HUMAN LENSES* P. SALIT, PH.D. Iowa City, Iowa A comparative study of the water content of cataractous and normal human lenses was evidently made first by Deutschmann.
some 60 years ago. In a previous publication 1 it was shown that there is a decrease in the phospholipid content of cataractous lenses, especially in the advanced stages of maturity. Since this is at variance with the older conception, according to which all lipids are supposed to show an increased amount in cataractous lenses, it was considered necessary to repeat the work.
In this study, total Ca 2+, K +, Na + and Mg 2+ contents have been determined in human normal and cataractous lenses using atomic absorption and flame emission spectroscopy.
The normal human lens Ca 2+ is between 015 and 05 μmol g ‐1 fresh lens weight; in senile cataracts the value increased up to 931 μmol g ‐1 (p. Studies using human lenses ^^^w^^^'^^-^'^^ Fig.
Transmission electron micrograph of female cataractous lens epithelial cells in culture. Note the large amount of collagen and basement membrane around the cell. Fig. Transmission electron micrograph of female cataractous lens epithelial cell in culture. cataractous lenses range 6 to 13 um when compared with the age matched control lenses where it was ± um (range 10 to 14 um).
This may be attributed to the decreased metabolic activity in cataractous lenses. Brown and Bron 6 measured the epithelial cell diameter um (range 8 to 21 um). Mizuno. A., Ozaki, Y. Itoh, K. and Matsuzaki. An application of laser Raman spectroscopy to the study of hereditary cataractous lens: on the Raman band for a diagnostic marker of cataractous signatures.
Curr. Eye Res. 2, Iwata, S. and Takehana, M. Biochemical study of human cataractous lens (fourth report) Acta Soc. Deamidation of proteins is one of the most prevalent post-translational modifications found upon aging, and in age-onset diseases. Specific asparagine and glutamine residues are often selectively deamidated during this process.
In the human lens, deamidation has been shown to occur in many crystallins, but it is not clear how these deamidated proteins lead to lens opacity or cataract. Here we. Aging research on the human eyes crosses all areas of ophthalmology and also relies upon biological, morphological, physiological, and biochemical tools for its study.
In Age-Related Changes of the Human Eye, the authors review all aspects of human eye aging. In addition to descriptions of age-related changes in almost all the structures of the. BIOCHEMICAL MEDICINE AND METABOLIC BIOL () Further Studies on Elastase and Trypsin Inhibitory Activities in Mammalian Lenses S.
SWAMINATHAN AND T. PATTABIRAMAN Department of Biochemistry, Kasturba Medical College, ManipalKarnataka, India Received J In an earlier communication from this laboratory (1).
Fig. 1B shows the IR spectra between and cm −sly, except the amide I bands (– cm −1) and glycogen bands (– cm −1), all the other bands are similar among the normal lenses and immature cataractous human lenses with or without maximum peaks of amide I bands atand cm −1 assigned to β-sheet structure were.
Abstract. When considering the biochemical causes of cataract, attention may be directed (1) to those types of change in lens morphology which may be designated an opacity, and (2) those biochemical derangements responsible for them. The study was carried out on patients with cataractous lens to isolate and characterize cartico capsular adhesion (CCA) molecules present in human senile cataractous lens and select a pharmacological base that can dissolve CCA in vivo and in vitro.
The activities of three enzymes which act on glucose, namely hexokinase, aldose reductase and glucose dehydrogenase, were measured in extracts of eye lens from cow, calf, rabbit, rat and guinea pig, and in human cataractous lenses. The K m (glucose) of these three enzymes in extracts of cow lens was found to be 012m m, 28m m and m m.
The accumulation of selenite in the lens may cause cataract formation and explains the high selenium content [19,20] in human lenses with increased opacity. Opaque lenses also show an accumulation of calcium [21,22].
An increase in intracellular Ca 2+ triggers calcium-activated enzymes such as calpains. Biochemical Studies on the Human Cataractous Lens. Author: Alao, J. Awarding Body: University of Salford Current Institution: University of Salford Date of Award: Availability of Full Text: Access from EThOS: Order from print.
A scan fee will apply. Phospholipids in proteolipids of each of these anatomic zones were quantitatively estimated and compared with that of different stages of human cataractous lenses.
In this study.A large volume of work has been done during the last four or five years in biochemical studies of the three refractive media of the eye: the aqueous, the lens and the vitreous. One wonders why such studies were not made earlier, and what are the chief factors .studies have indicated that it was increased .
LM was highly expressed in the capsules of cataractous lenses [32, 33]. Previous studies have demonstrated that the human adult lens capsule is composed of LMα5-α1, LMβ2-β1, and LMγ1 subunits .
The relationship between LM subunits and senescence was well studied in cells aside from LECs.