Problems of Scoliosis

Manning, Charles

doi:10.1136/bmj.2.5597.106

Cited by 7 publications

(15 citation statements)

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“…Lenses were classified as normal or cataractous as described by Anderson and Spector (12). Cataracts (14).…”

Section: Methodsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

“…The lens is composed primarily of protein which comprises most of the dry weight (7). It has been previously shown that the relative percentage of water-insoluble material increases with aging in both animal (8) and human (9-11) lenses and in the development of lens opacities (9)(10)(11) (14).The subunit polypeptides of 65-to 72-year-old cataractous lens protein were isolated from Sephadex G-150 and G-100 equilibrated with 10% HOAc and 7.2 M urea as described elsewhere (15). All polypeptides described were reduced and alkylated prior to their purification unless otherwise noted.…”

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confidence: 99%

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Racemization in human lens: evidence of rapid insolubilization of specific polypeptides in cataract formation.

Garner¹,

Spector²

1978

Proc. Natl. Acad. Sci. U.S.A.

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After early life, the dry weight of normal human lenses increases at a relatively constant rate with time.Transformation from soluble to insoluble material appears to occur at a comparable rate, resulting in a constant amount of soluble material. However, in cataract the insolubilization rate is accelerated. These observations are supported by determination of D-aspartic acid/L-aspartic acid ratios. The lens is composed primarily of protein which comprises most of the dry weight (7). It has been previously shown that the relative percentage of water-insoluble material increases with aging in both animal (8) and human (9-11) lenses and in the development of lens opacities (9)(10)(11) (14).The subunit polypeptides of 65-to 72-year-old cataractous lens protein were isolated from Sephadex G-150 and G-100 equilibrated with 10% HOAc and 7.2 M urea as described elsewhere (15). All polypeptides described were reduced and alkylated prior to their purification unless otherwise noted. RESULTS AND DISCUSSIONWhen the total dry weight (water-soluble plus water-insoluble) of normal lenses is plotted against age, after the first few years of rapid growth an increase in apparent weight of approximately 0.4 mg/yr is found (Fig. 1). Similar results have been observed by Klethi (17). Determination of the dry weight of the water-insoluble fraction suggests that it increases at the same rate as the total dry weight. Such observations indicate that the absolute amount of the water-soluble fraction remains constant at approximately 30 mg, and the rate of conversion of soluble to insoluble material is constant in the normal lens. Thus, the percentage of insoluble material increases at a constant rate from about 2% at birth to approximately 50% by about age 70 years.When individual cataractous lenses were examined (open circles in Fig. 1), the total weight generally corresponded (within experimental error) to that of normal lenses of the same age group. However, the amount of the water-insoluble fraction in the cataractous lenses (solid circles) was dramtically greater than in the normal lenses, suggesting a more rapid conversion of soluble to insoluble material. Thus, it would appear that a relatively rapid loss of water-soluble protein may be correlated with lens opacity.The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U. S. C. §1734 solely to indicate this fact.

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“…Lenses were classified as normal or cataractous as described by Anderson and Spector (12). Cataracts (14).…”

Section: Methodsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

mentioning

confidence: 99%

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Racemization in human lens: evidence of rapid insolubilization of specific polypeptides in cataract formation.

Garner¹,

Spector²

1978

Proc. Natl. Acad. Sci. U.S.A.

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“…Fortunately, amino acid analyzers employing ion-exchange chromatography for the separation and detection of amino acids 9 and derivatives 10 were common in peptide and protein chemistry laboratories. These instruments could also be used to separate and detect mixtures of small peptides, 11,12 thereby allowing the determination of relatively low-level side reactions (!0.1%) in model peptide systems. The model system used to detect possible amino acid insertions during SPPS 8 is illustrated in Figure 2.…”

Section: Amino Acid Insertions In Sppsmentioning

confidence: 99%

“…Glycine was employed since insertion reactions should be most favored in the absence of bulky side chains. Large excesses (11)(12)(13)(14)(15)(16)(17)(18)(19)(20)(21)(22) equiv) of Boc-Gly-OH and DCC were used to promote acylation of the peptide bond. An amino acid analyzer calibrated with H-(Gly n )-OH (where n ¼ 1 through 4) was used to detect the products obtained from the acidolytic cleavages (HBr-TFA) of peptide resin products 1 and 2.…”

Section: Amino Acid Insertions In Sppsmentioning

confidence: 99%

Studies in solid‐phase peptide synthesis: A personal perspective

Mitchell

2008

Biopolymers

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By the early 1970s it had became apparent that the solid‐phase synthesis of ribonuclease A could not be generalized. Consequently, virtually every aspect of solid‐phase peptide synthesis (SPPS) was reexamined and improved during the decade of the 1970s. The sensitive detection and elimination of possible side reactions (amino acid insertion, Nα‐trifluoroacetylation, Nαϵ‐alkylation) were examined. The quantitation of coupling efficiency in SPPS as a function of chain length was studied. A new and improved support for SPPS, the “PAM‐resin,” was prepared and evaluated. These and many other studies from the Merrifield laboratory and elsewhere increased the general acceptance of SPPS leading to the 1984 Nobel Prize in Chemistry for Bruce Merrifield. © 2007 Wiley Periodicals, Inc. Biopolymers (Pept Sci) 90:215–233, 2008.This article was originally published online as an accepted preprint. The “Published Online” date corresponds to the preprintversion. You can request a copy of the preprint by emailing the Biopolymers editorial office at biopolymers@wiley.com

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Synthesis of tritium-labelled isopenicillin N, penicillin N and 6-aminopenicillanic acid

Usher

Loder

Abraham

1975

Biochemical Journal

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1. Phenoxymethylpenicillin sulphoxide 4-methoxybenzyl ester was labelled with 3H in its 2-beta-methyl group. Its specific radioactivity was 362 mCi/mmol. 2. Removal of the side chain of this compound yielded the corresponding ester of 6-aminopenicillanic acid sulphoxide and coupling of the latter with the appropriate protected alpha-aminoadipic acid gave 4-methoxybenzyloxycarbonylisopenicillin N sulphoxide di-4-methoxybenzyl ester or the corresponding derivative of penicillin N. 3. Removal of the protective groups by hydrogenolysis and reduction of the sulphoxide group yielded 3H-labelled isopenicillin N or penicillin N. 4. 3H-labelled phenoxymethylpenicillin sulphoxide was obtained by hydrogenolysis from its 4-methoxybenzyl ester. Reduction of its sulphoxide group and subsequent removal of the side chain gave 3H-labelled 6-aminopenicillanic acid.

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Problems of Scoliosis

Cited by 7 publications

References 0 publications

Racemization in human lens: evidence of rapid insolubilization of specific polypeptides in cataract formation.

Racemization in human lens: evidence of rapid insolubilization of specific polypeptides in cataract formation.

Studies in solid‐phase peptide synthesis: A personal perspective

Synthesis of tritium-labelled isopenicillin N, penicillin N and 6-aminopenicillanic acid

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