Kettering University

About: Kettering University is a education organization based out in Flint, Michigan, United States. It is known for research contribution in the topics: RNA & Antigen. The organization has 6842 authors who have published 7689 publications receiving 337503 citations. The organization is also known as: GMI Engineering & Management Institute & General Motors Institute.

Erythropoietin derived by chemical synthesis.

Abstract: Erythropoietin is a signaling glycoprotein that controls the fundamental process of erythropoiesis, orchestrating the production and maintenance of red blood cells. As administrated clinically, erythropoietin has a polypeptide backbone with complex dishomogeneity in its carbohydrate domains. Here we describe the total synthesis of homogeneous erythropoietin with consensus carbohydrate domains incorporated at all of the native glycosylation sites. The oligosaccharide sectors were built by total synthesis and attached stereospecifically to peptidyl fragments of the wild-type primary sequence, themselves obtained by solid-phase peptide synthesis. The glycopeptidyl constructs were joined by chemical ligation, followed by metal-free dethiylation, and subsequently folded. This homogeneous erythropoietin glycosylated at the three wild-type aspartates with N-linked high-mannose sialic acid–containing oligosaccharides and O-linked glycophorin exhibits Procrit-level in vivo activity in mice.

Photoreduction of 2,6-Dichlorophenolindophenol by Diphenylcarbazide: A Photosystem 2 Reaction Catalyzed by Tris-Washed Chloroplasts and Subchloroplast Fragments

Abstract: The use of diphenylcarbazide as an electron donor coupled to the photoreduction of 2,6-dichlorophenolindophenol by tris-washed chloroplasts or subchloroplast fragments provides a simple and sensitive assay for photosystem 2 of chloroplasts. By varying the concentration of tris buffer at pH 8.0 during an incubation period it is shown that the destruction of oxygen evolution activity is accompanied by a corresponding emergence of an ability to photooxidize diphenylcarbazide, as evidenced by absorbance changes due to diphenylcarbazide at 300 nm. The temperature-sensitive oxidation of diphenylcarbazide is inhibited by DCMU and by high ionic strengths. This activity appears to measure the primary photochemical reaction of photosystem 2.

Capping Enzyme in Eukaryotic mRNA Synthesis

Abstract: Publisher Summary This chapter discusses the enzymatic mechanism of the individual capping reactions and the organization of the functional domains, within the relevant enzymes. Greatest attention is devoted to two model systems, Vaccinia virus and Saccharomyces cerevisim, in which biochemistry, molecular genetics, and protein engineering have fueled considerable progress, since the past review of ribonucleic acid (RNA) capping in this series. It also discusses the genetic studies in yeast that shed light on the physiologic role of the cap in eukaryotic RNA metabolism. Capping may serve to protect the messenger RNA (mRNA) from nucleolytic degradation. Elucidation of the mechanism and potential regulation of cap formation is, thus, pertinent to the understanding of eukaryotic gene expression. Capping occurs, by a series of three enzymatic reactions, in which the 5’ triphosphate terminus of a primary transcript is first cleaved to a diphosphateterminated RNA by RNA triphosphatase, then capped with GMP by RNA guanylyltransferase, and methylated at the N7 position of guanine by RNA (guanine-7) methyltransferase.

Chido and Rodgers blood groups are distinct antigenic components of human complement C4

Abstract: THE HLA complex consists of many closely linked genes which code for a variety of characters, particularly the expression of cell surface antigens found on lymphocytes (HLA-A, B, C, DR antigens) or erythrocytes (Chido and Rodgers blood groups) and polymorphic variation of certain complement components (Bf, C2, C4). We1 have recently suggested that the polymorphism of the fourth component of human complement (C4), detected by immunofixation electrophoresis, is controlled by two genes linked to HLA and not by codominant alleles at a single locus as previously described2,3. One C4 variant, designated F, is controlled by one locus with alleles determining the presence (F+) or absence (f0) of four fast-moving anodal bands of C4 while the second variant, S, is controlled by a second locus with alleles determining the presence (S+) or absence (s0) of four slow-moving cathodal bands. We noted that C4 F individuals homozygous for the s0 allele and lacking the four cathodal bands were always Chido (Cha) negative, whereas individuals homozygous for the f0 allele and lacking the four anodal bands of C4 (C4 S) were always Rodgers (Rga) negative. This intriguing observation led us to study the relationship of Chido and Rodgers red cell antigens, which are also found in serum and C4. We show here that Chido and Rodgers are distinct antigenic components of human C4, a finding which provides a biological explanation as to why these unique red cell antigens are controlled by genes of the HLA complex.