Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0029713 (immaturity)
 4,335 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The physiological protien and glycoprotein excretions in the urine samples of a larger group of newborn infants were separated according to the molecular weights by SDS polyacrylamide gel electrophoresis and compared with the protein excretions of older children. We found higher proportions of albumin, of high molecular weight (MW = molecular weight greater than or equal to 150 000 dt) and of lower molecular weight (MW less than albumin 6800 dt) proteins in the first 24-h urine samples after birth. One week after birth the low molecular weight proteins predominated because there was a substantial decrease in the excretion of albumin and of high molecular weight proteins (MW greater than or equal to 150 000 dt). We compared the patterns of protein excretion of the newborn infants with those of children aged from 2 1/2 to 15 years. These urines samples showed a typical pattern of protein excretion not correlated to the age. These findings express a transitory immaturity of the glomerular filter and of the tubular protein reabsorbing system of the newborn kidney. Apparently, the tubular protein handling normalizes later than the glomerular filtration of proteins.
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PMID:[Molecular weight analysis of physiological proteinuria in newborn infants (author's transl)]. 44 52

Ejaculated human spermatozoa were studied to assess their nuclear maturity. After SDS or SDS-EDTA treatment, asthenozoospermic semen had a lower resistance to decondensation than normozoospermic semen and contained more stained immature nuclei after aniline blue staining. It showed a higher uptake of ethidium bromide, specific for DNA. There was no difference in the binding of 14C iodoacetamide in the two groups. Therefore, asthenozoospermic semen could be characterized by its relative nuclear immaturity.
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PMID:Human spermatozoal nuclear maturity in normozoospermia and asthenozoospermia. 246 2

It was observed in the course of other studies that rat fetal lung extracts inhibited proliferation of fetal lung cells in culture. The purpose of the present study was to isolate and characterize this cytostatic factor. It was found that fetal lungs contained a 16 kDa cytostatic factor and its concentration was twofold greater in fetal lungs of diabetic rats compared with control rats. This fetal lung cytostatic protein (FLCP) was purified by reversed-phase, heparin-affinity and gel filtration high-performance liquid chromatography and SDS-PAGE. The purified protein was electroblotted onto polyvinylidene difluoride membrane and subjected to sequence analysis. The amino-terminal sequence of this fetal lung cytostatic protein was P E P A K S A P A P X K G I G K Q X X K A X X K A ... and showed significant homology with histone H2B; however, the amino acid composition of FLCP suggested that it may be structurally distinct from histone H2B. Ion-spray mass spectrometry suggested that FLCP was made up of at least two species of the protein with molecular weights of 13,776.1 and 14,007.3 and was different from the molecular weight of rat histone H2B predicted by its cDNA sequence. The concentration of FLCP, based on amino acid compositions, was 0.32 nmol/g and 0.83 nmol/g wet fetal lung from non-diabetic and diabetic rats respectively. These findings suggest that the fetal rat lung produces a regulatory factor bearing considerable homology with but possibly different from histone H2B and that fetal lung immaturity during diabetic pregnancy might be contributed to by an increase in this factor.
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PMID:Isolation and characterization of a cytostatic histone H2B-like protein from fetal lungs of non-diabetic and diabetic rats. 825 99