Repeated sequence elements in the high molecular weight basic nuclear proteins from the winter flounder

1987 ◽  
Vol 65 (10) ◽  
pp. 909-916 ◽  
Author(s):  
David C. R. Young ◽  
Peter L. Davies
Keyword(s):  
Molecular Weight ◽  
High Molecular Weight ◽  
Consensus Sequence ◽  
Repeated Sequence ◽  
Winter Flounder ◽  
Nuclear Proteins ◽  
High Pressure Liquid Chromatographic ◽  
Large Size ◽  
Sequence Elements ◽  
Liquid Chromatographic

In maturing sperm of the winter flounder, histones are not replaced by protamines but instead joined by a group of high molecular weight basic nuclear proteins. Despite their large size and number of components, these proteins were reduced to a relatively simple set of peptides by a "limit" digestion with endoprotease Lys-C. Nine of these peptides, that together account for half of the mass of the digest, were purified by two rounds of chromatography on a C18 reverse-phase high pressure liquid chromatographic column and analysed by sequential Edman degradation. Their sequences can be divided into two homology groups. Seven of the peptides contain all or part of a dodecapeptide consensus sequence, NH2-Ser-Pro-Met-Arg-Ser-Arg-Ser-Pro-Ser-Arg-Ser-Lys-COOH, which appears to be tandemly repeated. This dodecapeptide contains a previously recognized consensus phosphorylation sequence, NH2-Arg-Ser-Arg-Ser-Pro-COOH, in which both serines are phosphorylated during the early stages of spermiogenesis. The other homology group has the sequence NH2-Arg-Arg-Val-X-X-Pro-Lys-COOH, where X-X is either Gln-Thr or Pro-Ser. The dodecapeptide and heptapeptide sequences form at least 35 and 11%, respectively, of the high molecular weight basic nuclear proteins and are, therefore, repeated many times over in these proteins. A search for identical or homologous sequences within the Protein Sequence Database indicated that they are unique. The closest matches were to protamines and some viral DNA-binding proteins.

High Performance Liquid Chromatographic Analysis of Impurities and Degradation Products of Methoxychlor

1982 ◽  
Vol 65 (6) ◽  
pp. 1457-1470
Author(s):  
Paul R West ◽  
Sunil K Chaudhary ◽  
Graham R Branton ◽  
Reginald H Mitchell
Keyword(s):  
Molecular Weight ◽  
High Molecular Weight ◽  
Chromatographic Analysis ◽  
High Performance ◽  
Degradation Products ◽  
High Performance Liquid Chromatographic ◽  
Normal Phase ◽  
Chromatographic Techniques ◽  
Liquid Chromatographic Analysis ◽  
Liquid Chromatographic

Abstract Both reverse and normal phase high performance liquid chromatographic techniques have been applied to the analysis of technical methoxychlor. Facile detection of high molecular weight components yields information that is complementary to the gas chromatographic analysis of the technical pesticide and environmentally altered samples.

The mutation Ser511Asn leads to N-glycosylation and increases the cleavage of high molecular weight kininogen in rats genetically susceptible to inflammation

Blood ◽  
2003 ◽  
Vol 102 (8) ◽  
pp. 2835-2842 ◽  
Author(s):  
Irma Isordia-Salas ◽  
Robin A. Pixley ◽  
Hemant Parekh ◽  
Satya P. Kunapuli ◽  
Fengling Li ◽  
...  
Keyword(s):  
Molecular Weight ◽  
High Molecular Weight ◽  
Chronic Inflammation ◽  
Cho Cells ◽  
Single Point ◽  
Consensus Sequence ◽  
Chinese Hamster ◽  
Single Point Mutation ◽  
High Molecular Weight Kininogen ◽  
Molecular Alteration

Abstract Crohn disease is immunologically mediated and characterized by intestinal and systemic chronic inflammation. In a rat model, injection of peptidoglycan-polysaccharide complexes into the intestinal wall induced chronic inflammation in Lewis but neither Fischer nor Buffalo rats, indicating a differential genetic susceptibility. Proteolysis of plasma high molecular weight kininogen (HK) yielding bradykinin and cleaved HK (HKa) was faster in Lewis than in Fischer or Buffalo rat plasma. A single point mutation at nucleotide 1586 was found translating from Ser511 (Buffalo and Fisher) to Asn511 (Lewis). The latter defines an Asn-Xaa-Thr consensus sequence for N-glycosylation. We expressed these domains in Escherichia coli and found no differences in the rate of cleavage by purified kallikrein in the 3 strains in the absence of N-glycosylation. We then expressed these domains in Chinese hamster ovary (CHO) cells, which are capable of glycosylation, and found an increased rate of cleavage of Lewis HK. The Lewis mutation is associated with N-glycosylation as evidenced by a more rapid migration after treatment with N-glycosidase F. When CHO cells were cultured in the presence of tunicamycin, the kallikrein-induced cleavage rate of Lewis HK was not increased. This molecular alteration might be one contributing factor resulting in chronic inflammation in Lewis rats.

Microtubule motors and other maps

1990 ◽  
Vol 48 (3) ◽  
pp. 1-1
Author(s):  
Richard B. Vallee
Keyword(s):  
Molecular Weight ◽  
High Molecular Weight ◽  
Cytoplasmic Dynein ◽  
Organelle Transport ◽  
Structural Components ◽  
Microtubule Associated Proteins ◽  
Microtubule Motors ◽  
Associated Proteins ◽  
The Subject ◽  
Intracellular Motility

Microtubules are involved in a number of forms of intracellular motility, including mitosis and bidirectional organelle transport. Purified microtubules from brain and other sources contain tubulin and a diversity of microtubule associated proteins (MAPs). Some of the high molecular weight MAPs - MAP 1A, 1B, 2A, and 2B - are long, fibrous molecules that serve as structural components of the cytamatrix. Three MAPs have recently been identified that show microtubule activated ATPase activity and produce force in association with microtubules. These proteins - kinesin, cytoplasmic dynein, and dynamin - are referred to as cytoplasmic motors. The latter two will be the subject of this talk.Cytoplasmic dynein was first identified as one of the high molecular weight brain MAPs, MAP 1C. It was determined to be structurally equivalent to ciliary and flagellar dynein, and to produce force toward the minus ends of microtubules, opposite to kinesin.

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