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W Putt

Publications and source records attributed to W Putt.

34 records · Page 2Linked to original sources
PubMed1988

Complete sequence and in vitro expression of a tissue-specific phosphatidylinositol-linked N-CAM isoform from skeletal muscle.

Neural cell adhesion molecules (N-CAMs) are a family of cell surface sialoglycoproteins encoded by a single copy gene. A full-length cDNA clone that encodes a nontransmembrane phosphatidylinositol (PI) linked N-CAM of Mr 125 x 10(3) has been isolated from a human skeletal muscle cDNA library. The deduced protein sequence encodes a polypeptide of 761 amino acids and is highly homologous to the N-CAM isoform in brain of Mr 120 x 10(3). The size difference between the 125 x 10(3). The size difference between the 125 x 10(3) Mr skeletal muscle form and the 120 x 10(3) Mr N-CAM form from brain is accounted for by the insertion of a block of 37 amino acids called MSD1, in the extracellular domain of the muscle form. Transient expression of the human cDNA in COS cells results in cell surface N-CAM expression via a putative covalent attachment to PI-containing phospholipid. Linked in vitro transcription and translation experiments followed by immunoprecipitation with anti-N-CAM antibodies demonstrate that the full-length clone of 761 amino acid coding potential produces a core polypeptide of Mr 110 x 10(3) which is processed by microsomal membranes to yield a 122 x 10(3) Mr species. Taken together, these results demonstrate that the cloned cDNA sequence encodes a lipid-linked, PI-specific phospholipase C releasable surface isoform of N-CAM with core glycopeptide molecular weight corresponding to the authentic muscle 125 x 10(3) Mr N-CAM isoform. This is the first direct correlation of cDNA and deduced protein sequence with a known PI-linked N-CAM isoform from skeletal muscle.

Amino Acid Sequence↗
PubMed1987

Human muscle neural cell adhesion molecule (N-CAM): identification of a muscle-specific sequence in the extracellular domain.

cDNA clones encoding neural cell adhesion molecule (N-CAM) mRNAs of 6.7, 5.2, and 4.3 kb from human skeletal muscle cells were isolated. A 6.7 kb mRNA encodes a transmembrane N-CAM isoform, present predominantly in mononucleate myoblasts, that shows sequence homology with chick brain N-CAM-140 and is down-regulated during myotube formation. In contrast, the 5.2 and 4.3 kb mRNAs encode nontransmembrane N-CAM isoforms that greatly increase during myoblast fusion. Furthermore, a discrete muscle-specific sequence domain (MSD1) was detected in the extracellular coding regions of the 5.2 and 4.3 kb mRNAs. This encodes a unique run of 37 amino acids and is not expressed in 7.2 and 6.7 kb mRNAs from human or chick brain or in the corresponding 6.7 kb muscle transcript. The MSD1 is also absent from chick and mouse brain mRNAs of 4.0 and 2.9 kb. These results show that diversity in N-CAM primary structure can be found in the extracellular domain in a tissue-specific manner.

Amino Acid Sequence↗
PubMed1985

Chromosome mosaicism in a zebra (Equus burchelli) abortus provides evidence for a different in-vivo/in-vitro survival of balanced and unbalanced karyotypes.

A fibroblast culture from the skin of a zebra abortus recovered from a pedigree known, in part, to be segregating for a chromosome centric fission was karyotypically mosaic. Some cells were balanced for the fission and the others unbalanced, being deficient for the shorter fission product. Initially, the latter were in the majority but after continued culture (101 days) they were outgrown by the former. This finding either suggests a differential in-vivo/in-vitro fitness of the two cell types or a change in proportions resulting from some other mechanism.

Abortion, Veterinary↗
PubMed1983

Genetics of four plasma protein loci in Equus przewalskii: new alleles at the prealbumin, postalbumin and transferrin loci.

This paper reports genetic variation at the prealbumin (Pr), postalbumin (Pa) and transferrin (Tf) loci in Equus przewalskii found using thin layer isoelectric focusing and an amphoteric separator. The method resolves all three loci plus serum esterase (Es) on a single gel, and typing of all four loci is readily achieved. In addition to the esterase alleles previously reported by Fisher & Scott (1979), five alleles were found at the Pr locus, three at the Pa locus and six at the Tf locus. Analysis of several mating types confirms inheritance is autosomal and codominant for all four loci.

Alleles↗
PubMed1983

Immunological detection of the sixth complement component (C6) following flat bed polyacrylamide gel isoelectric focusing and electrophoretic transfer to nitrocellulose filters.

A method for the electrophoretic transfer of C6 molecules to a nitrocellulose filter is described. The protein is detected by the use of anti-C6 antibodies and a peroxidase conjugated antibody. Using this method typical isoelectric patterns of C6 variant phenotypes are found. Inheritance and population data are presented. Three rare structural variants, one of which appears to be previously unreported, were discovered among a sample of 202 individuals. The method is discussed from the viewpoint of its flexibility and its value as an additional tool for revealing inherited variations in structural gene products.

Antibodies↗
PubMed1979

An investigation of seven enzymes as possible genetic markers in horse leucocytes.

In this paper we describe seven enzymes, NP, GOTM, PGM2, alpha FUC, PEP A, ADA and MPI which are found in the white cells of horses, including 39 British crossbred ponies and 16 crossbred horses, 30 Mongolian ponies and 10 Icelandic ponies. Two of these enzymes--alpha FUC and MPI--were polymorphic in all the populations of horses studied and could prove useful as additional markers in the paternity testing of horses. PEP A and GOTM were also polymorphic in two of the populations studied and could be used as further markers in these populations.

Adenosine Deaminase↗
PubMed1978

An examination of the age-related patterns of decay of acid phosphatase (ACP1) in human red cells from individuals of different phenotypes.

A study has been made of the decay of acid phosphatase (ACP1) in the human red cell using red cell fractions of different mean ages prepared by density gradient centrifugation. Red cells from acid phosphatase type A and type B individuals were used in the study. Acid phosphatase activity of the red cell fractions was determined by two different assay methods. The results obtained were comparable and have been combined. Acid phosphatase type A and type B showed a biphasic decay pattern with a rapid early loss of activity, followed by a more gradual rate of decline. Type A appeared to decay more rapidly than type B in both decay phases. It is proposed that differences in stability between type A and type B in vivo may explain the observed differences in activity between the enzyme types. There was no evidence for the generation of secondary isozymes by acid phosphatase type A or type B during red cell aging.

Acid Phosphatase↗
PubMed1977

An interpretation of human diaphorase isozymes in terms of three gene loci DIA1, DIA2 and DIA3.

NADH and NADPH diaphorase isozymes have been studied in human tissues. Evidence from rare heterozygotes suggests that the red cell and main tissue forms of NADH diaphorase are products of the same locus DIA1. NADPH-dependent diaphorase appears to be the product of a second locus DIA2. A third locus, DIA3, codes for the polymorphic sperm diaphorase. The products of this locus are also found in foetal tissues including placenta and adult brain and gonads. The products of these three loci may be distinguished by their substrate specificity, thermostability and molecular size.

Adolescent↗
PubMed1977

The distribution of isoelectric points of human soluble proteins and in particular of the enzyme products of 88 human gene loci.

The isoelectric points of the 'primary' isozymes coded for by 88 human gene loci have been determined. The distribution was found to be bimodal with an antimode at the 'physiological pH'. Soluble human proteins have the same distribution and this appears to be characteristic of soluble mammalian proteins in general. There may be some correlation with function, mitochondrial enzymes being more basic and hydrolytic enzymes being more acidic than other classes of enzymes. The bimodal distribution can be explained in terms of the buffering effects of the charged amino acids. Most proteins would thus appear to be charged at neutral pH values.

Alleles↗