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Biomedical subjects

D V Kosiagin

Publications and source records attributed to D V Kosiagin.

17 recordsLinked to original sources

[Fractionation of urinary glycosaminoglycans using ethanol, their purification and study].

A new method for the isolation of the urine glycosaminoglycans (GAG) with the use of ethanol is suggested. Experimental conditions for ethanol sedimentation and purification of GAG have been selected. It is suggested that the urine GAGs be divided into sulfated and nonsulfated with the use of resochin and their uronic acids and hexoses be examined. The normal GAG level and composition in humans have been determined.

Chemical Fractionation↗

[Mathematical relationship between the dimensions of the auditory ossicles and fetal age].

Having applied morphometric data obtained on more than 400 auditory ossicles from prefetuses and fetuses at different stages of intrauterine development, the dynamic changes of the greatest size of the malleus, incus and stapes were investigated in age aspect. Increase in size of the auditory ossicles was stated to occur unevenly, every bone having certain periods of the most intensive growth. Mathematical relation of the auditory ossicles growth has been revealed and presented graphically, in an equation. This relation makes it possible to establish mathematically the dementions of the auditory ossicles at any stage of their development. And, according to the auditory ossicles dementions, it is possible to ascertain the fetus age, the data useful for medicolegal practice.

Ear Ossicles↗

[Glycosaminoglycans in tissue forming joint elements].

A method is suggested to isolate and purify glycosaminoglycans forming elements of a joint from different kinds of connective tissue. The suggested method has been used to study the amount and composition of glucosaminoglycans in the knee joint tissues of people who had died from different accidents. The cartilage of patella and medial condyle of the femur, synovial membrane, medial meniscus and medial tendon of musculus quadriceps femoris are studied. Differences in the amount and composition of glucosaminoglycans in adults are shown.

Adult↗

[The length of chondroitin sulfate chains in normal and degenerative cartilage].

Content of chondroitin sulphate, the number and average length of its chains are studied in isolated glycosamineglycanes from unchanged and degeneratively changed cartilage in men of different age. The chondroitin sulphate amount in the cartilage tissue is shown to decrease without change in the number of its chains with the age and with the development of the degenerative process in the cartilage. It occurs as a result of shortening of the average length of chondroitin sulphate chains which can be induced either during atypical chondrocyte synthesis of proteoglycanes or under destruction of the latter by enzymes.

Adolescent↗

[The ratio of protein and carbohydrate components of proteoglycans from normal and degenerative articular cartilage].

The protein/uronic acid ratio in monomers and aggregates of proteoglycans in the human articular cartilage is investigated. It is shown that for the first two hours of cartilage extraction by isotonic solution proteoglycans with the low concentration of chondroitin sulphate are mainly removed; in the process of the subsequent extraction proteoglycans with a large amount of chondroitin sulphate; the quantity of chondroitin sulphate in the molecule does not effect the ability of proteoglycans to aggregation. The protein/uronic acid ratio increases in cartilage proteoglycans with aging and in the process of cartilage degeneration due to a decrease in the amount of the carbohydrate part of the molecule.

Adult↗

[Glycosaminoglycan levels in normal and degenerative articular cartilage of people of different ages].

Content of glycosaminoglycans in normal and degenerative joint cartilage of various old persons from birth up to senile age was studied by means of estimation of uronic acids, hexoses and hexosamines. In normal cartilage content of hexosamines did not alter with age but concentration of uronic acids was gradually decreased especially distinct at the senile age. Content of hexoses was increased from birth up to 35 years old age and then it was decreased. In degeneratively impaired cartilage content of glycosaminoglycans was decreased; content of all three carbohydrates studied was lesser in the impaired cartilage as compared with normal tissue from persons of the same age.

Adolescent↗

[Amino acid composition of proteoglycan protein of human articular cartilage in normal conditions and in degeneration].

Proteoglycan protein of human articular cartilage is found to contain a considerable amount of leucine, proline, glutaminic acid and glycine. The amino acid composition of various proteoglycan fractions differs in the methionine content. Proteoglycan protein from the degeneratively changed cartilage contains a less amount of lysine and serine. It is supposed that the found changes may be induced by the atypical synthesis of the proteoglycan protein shaft by chondrocytes under the cartilage degeneration.

Amino Acids↗

[Human articular cartilage proteoglycans extracted by salt solutions].

Studies were performed to investigate the capacity of proteoglycans for being extracted by salt solutions from unchanged and degeneratively changed articular cartilage of children and people of mature and elderly age. The content of proteoglycans and capacity for extraction depend on the age and degenerative changes in the cartilage tissue.

Adult↗

[Proteoglycans of human articular cartilage normally and in age-related degenerative changes].

Content of proteoglycans (PG) was decreased in human joint cartilage under degenerative conditions. This decrease occurred mainly due to the PG tightly bound with collagen but not of their monomers as shown by a stepwise extraction of the PG fractions. Fraction of the PG aggregates, not bound with collagen, was relatively increased in degeneratively impaired cartilage; this appears to occur as a result of impairment in reaction of the PG molecules with collagen matrix.

Adult↗

[Modification of the method for isolating proteoglycan fractions from cartilage tissue].

A method is suggested for isolating proteoglycans from cartilage tissue with their simultaneous separation into fractions. A successive treatment of cartilage with solutions of different salts and papain produced proteoglycans monomers with short and long chains of glycosaminoglycans, proteoglycans aggregates free and bound with collagen. The content of proteoglycans fractions in the unchanged and degeneratively changed human articular cartilage is determined, the results are given. The data obtained by the method suggested are comparable with the results by other determination methods. The method is technically simple and may be applied for the analysis of the operation and section material.

Cartilage↗